On top of this, ebooks are very convenient for the readers buying them. Buying a physical book involves going to a bookstore and hoping they have it in stock, or ordering it online and waiting for it to arrive. For ebooks, you go to a website, click the "Buy" button, and download the book to your PC or reader.
Are people willing to pay for convenience?
This constraint is the reason ebooks sometimes cost more than paperbacks. For example, a publisher can list the price of their physical book at $27.95 and the ebook at $20, which is a reasonable 30 percent markdown.
Explain why ebooks sometimes cost more than physical books.
Unlike with physical books, Amazon has no control over the price of ebooks. If someone has performed the steps required to publish an ebook via Kindle Direct Publishing, they set the price as they please, with no exceptions.
Do you think this is true for authors who don't have a following?
However, ebooks utilize the agency model when sold. Instead of letting the retailer choose the price, the publisher states what they're selling for. The publisher gets 70 percent of each transaction, and the retailer gets the remaining 30 percent.
How is the pricing system for ebooks different from the one for physical books?
Everything makes sense when you imagine all of the people who helped make the book who need paying. For one, the author has to get their agreed royalty cut from every sale. From there, the editors, proofreaders, cover artists, and marketers all need to be paid. These obligations don't leave the publisher with a lot of money for themselves.
Who else needs to be paid besides just the author?
a physical book takes around $1-2 to produce. If this is true, however, then why are they priced a lot more than that?
Does this surprise you?
Great list! Some things we didn't think about until we needed them are:
Why do we need this proprietary service?
So they can track us when we go to: http://svelte-autocomplete.surge.sh/?ref=madewithsvelte.com ?
Rather than bookmark/use https://madewithsvelte.com/svelte-autocomplete I would prefer to just use https://github.com/elcobvg/svelte-autocomplete as the canonical URL for this project.
címkefelhő
tag cloud
Címkefelhő
tag cloud
tag cloud
Jelentése: kulcsszavak vizuális ábrázolása
(tag cloud
kulcsszavak vizuális ábrázolása
Oh, and from a language/design perspective, you can actually turn regular words in a sentence into channels, just as many people do with @replies. For example: I’m coming to #barcamp later today.
Because the use of hashtags is inline and you can turn regular words into hashtags (and therefor channels), there is no friction to do so.
It also enforces actual use in the wild of tags, since no evidence of a tag will exist without it first being used in conversation. This means that representing channels in tagclouds across the site that grow and fade over time, and are contextual to all of Twitter or to a single user, is the ideal interface for displaying this information.
Hashtags have the added benefit that they won't show up for others if they're not used.
If you look at which hashtags are being used (trending), you get a taxonomy of micro-contexts, ranked by popularity, with which you can navigate Twitter. All from the bottom up.
I also like that the folksonomic approach (as in, there are no “pre-established groups”) allows for a great deal of expression, of negotiation (I imagine that #barcamp will be a common tag between events, but that’s fine, since if there is a collision, say between two separate BarCamps on the same day, they’ll just have to socially engineer a solution and probably pick a new tag, like #barcampblock) and of decay (that is, over time, as tags are used less frequently, other people can reuse them — no domain squatting!).
The folksonomic approach (user-generated tagging) is beneficial because it allows complexity to emerge bottom-up.
Every time someone uses a channel tag to mark a status, not only do we know something specific about that status, but others can eavesdrop on the context of it and then join in the channel and contribute as well. Rather than trying to ping-pong discussion between one or more individuals with daisy-chained @replies, using a simple #reply means that people not in the @reply queue will be able to follow along, as people do with Flickr or Delicious tags. Furthermore, topics that enter into existing channels will become visible to those who have previously joined in the discussion. And, perhaps best of all, anyone can choose to leave or remove topics that don’t interest them.
Twitter's hashtags form a dual purpose. They label a status with a certain tag, telling us something about the intended context of that Tweet.
The ease of which makes it frictionless for anyone to jump into the conversation.
But they also equip an interested eavesdropper with the ability to follow along with a conversation. This idea (at the time this was being discussed at Twitter) was already happening with Flickr and Delicious tags.
This is how it works in IRC, and how it needed to work in Twitter.
The idea of:
When you use a hastag and the channel with that name doesn't exist, it gets created, is an idea that came from IRC.
Now, in thinking about implementing channels, it was imperative that I not introduce any significant changes into the way that I currently use Twitter any more than I have for other features that have been added to Twitter (for example, @replies or direct messages). Channels would need to be a command-line-friendly addition, and one that would require absolutely zero web-based management to make the most of it (to draw a distinction, Pownce fails this test with its Friend Sets, since it requires use of their website to take advantage of this feature).
The requirements [[Joe Messina]] laid out for a concept of "channels" on Twitter was that:
Twitter of 2020 satisfies these requirements. You just type #something, and you can click on that hash or search for it to see results.
Jaiku comes closest with their channels implementation, making it extremely easy to create new channels (simply post a message that begins with a hash (#) and your intended channel name — and if the channel doesn’t exist, it’ll be created for you):
[[Joe Messina]] details an example from [[Jaiku]] where you can create a channel by simply posting a message that starts with a hash (#). If the channel doesn't exist, it will be created for you.
I’m more interested in simply having a better eavesdropping experience on Twitter.
[[Joe Messina]]'s reason for suggesting the hashtag was his interest in having "better eavesdropping experience on Twitter"
SGML
Az SGML (Standard Generalized Markup Language, szabványos általános jelölőnyelv) egy ISO szabványos jelölőnyelv dokumentumformátumok leírására. Az SGML elődjét, a GML-t (Generalized Markup Language) az 1960-as években fejlesztette ki az IBM-nél Charles Goldfarb, Edward Mosher és Raymond Lorie (családnevük kezdőbetűi alapján találta ki Goldfarb a GML nevet). Ennek leszármazottja az SGML, ami 1986-ban lett ISO ( International Organization for Standardization) szabvány.[1]
Az SGML egy absztrakt szintaxist biztosít, amit sokféle alkalmazásban használhatunk. A szabványos szintaktika lehetővé teszi, hogy az ilyen formátumú dokumentumokat egy általános célú értelmezővel (parser) könnyen beolvashassuk, írhassuk vagy formailag ellenőrizhessük. SGML-ben a jelölések (tag) jelentése nincs meghatározva, ez mindig az SGML-t használó alkalmazás feladata (például a HTML-ben, ami az egyik legismertebb SGML alkalmazás, a jelöléseknek már konkrét jelentésük van, és a jelölések értékkészlete véges).
anti-HA
DOI: 10.1016/j.celrep.2020.108332
Resource: (Cell Signaling Technology Cat# 3724, RRID:AB_1549585)
Curator: @Naa003
SciCrunch record: RRID:AB_1549585
Curator comments: Rabbit Anti-HA-Tag Monoclonal Antibody, Unconjugated, Clone C29F4 Cell Signaling Technology Cat# 3724
Nutrition
practicing
Schulprogramm (wird überarbeitet)
Muss vor dem Tag der offenen Tür auf jeden Fall da hin ;-). (Note to myself)
Did you look at it and decide not, or not look at it?
This isn't written to hype a battle in the holy war.
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Ignoring official advice
See: https://github.com/sveltejs/svelte/issues/5158
I also tried to use
<!-- svelte-ignore unused-export-let -->before thescripttag but still no chance.
I also tried to use <!-- svelte-ignore unused-export-let --> before the script tag but still no chance.
As of version 3.5.2 and #3013, attributes that are set to null or undefined won't be added to the tag.
group: Ariel Methodology Group Narrow your search: user: search by username tag: search for annotations with a tag url: search by URLfor domain level search add trailing /* eg. example.com/* group: show annotations associated with a group Danfff1
test note
test note
And that’s because to treat graphic design like it’s a service, where it makes sense to optimize time and labor for maximum efficiency, undermines the aura of indispensability, superiority, and yes, authenticity that institutions such as design schools and “professional associations” rely on in order to justify the massive dollar signs they place on themselves via tuition, and member fees.
I'm assuming Libby means that Rob Giampietro is on the other side of the argument where viewing design as something to be optimized for efficiency undermines that high dollar price tag that institutions have marketed as only possible by studying with them. But she is on the side that, that thinking is irrelevant to how design ought to progress.
http://jonudell.info/h/tag-rename-02.mp4
Most people would embed a YouTube video. Nice to see no dependency on 3rd-party service here.
The submission system required students to manually enter all ‘‘tags’’ (rele-vant topic keywords) for their letters, entering up to five tags per letter; thesystem did not provide a menu list of common issues for students to choosefrom.
I like that the tags were student generated. Personally, when given a list to choose a tag from sometimes I don't feel the tag is listed that is most appropriate. I enjoy that students were able to create their own tags to summarize the main issue of their letter.
For example, Samuel H. chose a "classroom" tag that peaked my interest. I was curious to explore what issues in the classroom he believed should be addressed. This is one of the aspects that stood out to me.
Looking at all those bearing, heading, orientation, navigation, position, direction, etc. I think we have a bigger problem here. Someone has decided how to use tag (e.g. orientation is about page orientation), but there are 100 other cases. Imho, to disallow misusing there should be no "heading", but rather "html-heading", "gps-heading", "whatelse-heading", which make mistakes impossible. So yes, "heading" should go.
Retagging the HTML/CSS questions to use html-heading seems the right thing to do. For the other uses, I don't have enough grounding in the geographic area to know whether the direction and bearing are replacements for heading. But the tag information for heading should be created and should firmly point at the other tags — at least until it is expunged.
Wurde beispielsweise ein Algorithmus zur Erkennung von Hautkrankheiten an Bildern isländischer Patienten trainiert, wäre das eine wichtige Information, da der Algorithmus womöglich bei australischen Ureinwohnern eine völlige andere Trefferquote an den Tag legt.
Welche Rolle spielt das Training von Algorithmen? Wie funktioniert es?
H3K14ub is a histone modification that facilitates deposition of H3K9me on heterochromatin in fission yeast, but the mechanism by which this modification stimulates Clr4 was unknown. Using mutants and HDX, the authors identified the interaction surface of Clr4 for H3K14ub, which they used to design mutants that responded poorly to H3K14ub stimulation. In vivo, these mutations resulted in loss of heterochromatin marks and defects in heterochromatin-based silencing, suggesting that H3K14ub stimulation is essential to K9me-mediated silencing. Finally, the authors show that human SUV39H2 but not G9a or Arabidopsis SUVH4 can be stimulated by H3K14ub in a similar manner.
The authors provided biochemical and structural insights into the mechanism that increases the H3K9-specific methyltransferase activity of Clr4 by H3K14ub. Although H3K14ub-mediated promotion of H3K9 methylation is shown in Oya et al. EMBO Rep 2019, this study further characterizes the potential mechanism. However, there are some issues with the results that need to be resolved.
1) Similarity and difference with the previous study. As the authors acknowledge, this manuscript builds on a previous study by Oya et al. 2019, however I think the similarities and the differences need to be made even more explicit and better addressed.
a) The authors should clearly state that Figure 1B and 1C are basically a confirmation of Oya et al. 2019.
b) I am more puzzled by the difference in the mapping of the region required for H3K14ub stimulation. The authors suggest that a difference in the preparation of the recombinant proteins might be responsible. This can and should be tested as it would seemingly be a simple experiment (compare with and without GST tag).
c) Possibly to reconcile their findings with the previous report the authors state in the description of Fig. 1 that "the N-terminus plays a regulatory role in the sensing of H3K14ub by the catalytic domain" but I don't see this reflected in the data show in Fig. 1C, given that the degree of stimulation is very similar for KMT and FL.
2) Stimulation-defective mutants. The authors should carefully discuss the stimulation-defective mutants, which should be premised on the retention of their methyltransferase activity on unmodified H3. The authors claim that 30% loss of activity of the Clr4 KMT mutants on unmodified H3 is observed in Figure S3C (Pg 11 line 15), but this cannot be determined from the graph provided, which is normalized to unmodified H3. The authors should (1) make another graph to show the 30% loss and (2) compare Clr4 KMT mutants with catalytic-dead Clr4 KMT or dissolution buffer (no protein). It is still possible that GS253 and F3A mutations simply reduce MTase activity, thus displaying lower activity than WT in the presence of H3K14ub, which would also suggest a different interpretation for the results in vivo.
3) Heterochromatin localization of Clr4 mutants. The FLAG ChIP results in Fig. 4E is not very informative, as with the loss of heterochromatin a loss of Clr4 is predicted. If the authors want to test whether the localization activity of Clr4 mutants is intact, (1) FLAG ChIP in the clr4+, Flag-Clr4GS253/F3A background (i.e., two clr4 alleles exist) or (2) in vitro H3K9me2/3 binding assay should be performed. Since Clr4 N-terminus might regulate MTase activity as discussed in Pg 18 line 19, it is also possible that amino acid substitutions in the KMT region affect the function of N-terminus, including CD. The co-IP in Fig. 4C is not sufficient to clarify this point as Clr4 directly binds heterochromatin via its CD, in addition to the CLRC-mediated mechanism, and it is unclear if this is affected in the mutants.
4) Allosteric vs. binding regulation. On Pg. 11, the authors suggest that an allosteric mechanism is at play, but this is not supported by the data. In fact the observation that providing ubiquitin in trans does not stimulate and rather inhibits the activity on H3K14ub would suggest that the ubiquitin just increases binding affinity. To clarify this the authors should measure binding affinity of WT and mutants to the H3 peptide with and without ubiquitin.
This manuscript further characterizes the role of HILPDA/HIG2 in TAG/LD biology. The major finding is that HILPDA interacts with and promotes DGAT activity and TAG synthesis, which is novel given that HILPDA has largely been thought to regulate TAG turnover as a lipolytic inhibitor.
Characterization of the interaction between HILPDA and DGAT1 (and to a lesser extent DGAT2) is the major strength of this paper and an important advancement in the field. The early parts of the paper are not particularly novel (Fig. 1) or well-designed (Fig 2. - poor NAFLD/NASH model showing almost no effects) and the study is a bit on the thin side for data.
1) The data shown in Figure 1 is not particularly striking given that HILPDA is a known target gene of PPAR-alpha, which is activated by FAs. Showing that HILPDA expression tracks with PLIN2 is also pretty obvious as PLIN2 tracks with LD accumulation. I really don't see the need/relevance of this figure.
2) The MCD diet is widely regarded as a poor model for NAFLD/NASH since it doesn't replicate human NASH in so many regards. As a result, the use of this model makes these studies less relevant. Also, it is referenced that HILPDA was found to be up in a MCD study, but why not look at the plethora of human and mouse studies of NAFLD that have done RNAseq or arrays to provide a more physiological assessment of its expression in NAFLD/NASH?
3) The conclusion that effects are independent of ATGL are not overly convincing. Since ATGListatin is not specific for ATGL (Quiroga et al. 2018), a more thorough and quantitative analysis of TAG turnover with ATGL knockdown/out is warranted if these claims are to be made.
4) Since DGAT1 mRNA is unchanged but protein goes up, it would be assumed that HILPDA is affecting DGAT1 stability/turnover. This should be considered.
This study dissects the role of LD associated protein HILPDA in triglyceride and LD homeostasis in hepatic tissue. Using a mouse tissue-specific HILPDA KO, live cell imaging, and lipid analysis, it proposes that HILPDA promotes TAG storage in LDs independently of ATGL regulation. Instead, HILPDA is proposed to interact with DGAT1 and promote TAG synthesis/storage.
This is an interesting and potentially exciting study that provides a new insight for HILPDA in liver fat storage. The proposed model differs from previous literature that proposes HILPDA regulates lipolysis via ATGL. Unfortunately, while the data presented support a potential role for HILPDA in DGAT regulation, a clear mechanism is not identified. The first half of the paper that phenotypes loss and over-expression of HILPDA is thorough and conclusive. The latter half of the paper, investigating the interplay between HILPDA and DGAT1, appears more preliminary.
The critical issue in this study is that the nature of the HILPDA-DGAT1 interaction is not well defined. HILPDA over-expression is shown to increase DGAT1 protein levels, but the specific mechanism underlying this is not further dissected. Furthermore, it is still unclear whether this interaction is direct, or merely stochastic due to the fact that both DGAT1 and HILPDA reside on the same LDs in the experiments presented. More biochemical investigation as to whether these proteins physically interact in their native states, and if so whether that interaction affects DGAT1 enzymatic activity directly or allosterically, is required. Without this the study is mainly descriptive.
Major concerns:
1) Fig 4: overnight and acute fatty acid addition experiment: The authors propose that HILPDA enriches at sites where new fatty acids are being processed. Can you demonstrate that both these fluorescent FA species are even being incorporated into TAG during the time periods associated with the microscopy? An alternative explanation is simply that HILPDA localizes to regions of the cell where FA esterification or incorporation into other lipid species is occurring. TAG is potentially only one of many fates for these FAs. Can DGAT1/2 be colocalized with HILPDA in these experiments? Alternatively, what happens in these experiments if DGAT inhibitors are co-added with the FAs?
2) Fig 5H: The DGAT activity assays indicate that HILPDA over-expression increases the incorporation of fluorescent FA and DAG into TAG, but it is unclear as written whether these assays are normalizing for DGAT1 protein amount. Does HILPDA over-expression enhance DGAT enzymatic activity in this panel, or merely promote TAG synthesis here by the increased total DGAT protein level noted later in the study? This is a clear distinction in mechanism, and needs to be dissected further.
3) Fig 6/7: DGAT1-HILPDA interaction. The data presented in Fig 7 indicate that DGAT1 and HILPDA co-localize in cells and potentially are in very close proximity with one another. However, the data as presented are not enough to indicate whether these proteins directly interact. Do these proteins immunoprecipitate with one another? Some biochemical evidence for their interaction is necessary
4) Fig 7: relatedly, the mechanism by which DGAT1 is increased in protein level from HILPDA is also unclear. Is the protein more long-lived, or stabilized in the ER when HILPDA is over-expressed? Again, protein biochemical analysis would be helpful.
This preprint was reviewed using eLife’s Preprint Review service, which provides public peer reviews of manuscripts posted on bioRxiv for the benefit of the authors, readers, potential readers, and others interested in our assessment of the work. This review applies only to version 2 of the manuscript.
This study further characterizes the role of lipid droplet (LD) associated protein HILPDA in LD biology. The authors propose that HILPDA promotes triglyceride (TAG) storage in LDs by a mechanism independent of ATGL, through activation of DGAT. This is a potentially interesting finding, however, as detailed by the reviewers below, the data presented do not identify a mechanism for how HILPDA affects DGAT.
We could broadcast a warning if we find the variable to be set in the environment, but that is more likely than not to annoy people who intentionally set it.
New tag?: warnings that may annoy people who intentionally do something. (Need a way to selectively silence certain warnings?)
Malicious code pushed to your .gitlab-ci.yml file could compromise your variables and send them to a third party server regardless of the masked setting. If the pipeline runs on a protected branch or protected tag, it could also compromise protected variables.
With over 1,500 dating apps on the market, many have come to the conclusion that the romance of courtship has been replaced with fantasy and heavily-edited Instagram photos. Along with driving this increase in dating apps, the millennial generation is also delaying marriage and moving away from conventional religious practices. Because of this, many popular magazines and TV shows suggest that hook-up culture dominates contemporary pursuits of love. Right-swiping, label free, highly educated, and technologically savvy, today’s young people appear to pursue sex frequently and do so on their own terms. There also appears to be much more equal footing between genders than ever before.
This is true, young generation does not want to bound themselves in a permanent relationship tag because now they have lots of options due to dating apps.
Although Madisyn applied only one tag of ‘‘Race’’ and did nottag her letter with ‘‘Police,’’ ‘‘Violence,’’ or anything else, her letter speaksto students’ deep and related concerns around discrimination, violence,and specifically the role of police.
This is observed in two of my letters too. Although the students tag their letters to one topic, they talk about other related issues. For example, in Vivian's letter "Problems in education", she talks about equity in education, standardized testing, and teacher pay. Her letter speaks to deeper and broader issues in education. - Anitha
BIO
gold data: IOB(inside-outside-beginning) format or BIO
quote from this link https://towardsdatascience.com/named-entity-recognition-and-classification-with-scikit-learn-f05372f07ba2
The IOB (short for inside, outside, beginning) is a common tagging format for tagging tokens. I- prefix before a tag indicates that the tag is inside a chunk. B- prefix before a tag indicates that the tag is the beginning of a chunk. An O tag indicates that a token belongs to no chunk (outside).
THE BOOK OF TEA By Kakuzo Okakura
Hi Bob!! 👋
Storyboard_cursoID
mouse anti‐DDDDK‐tag
DOI: 10.1111/acel.13251
Resource: (MBL International Cat# M185-3, RRID:AB_10950447)
Curator: @Naa003
SciCrunch record: RRID:AB_10950447
Curator comments: anti-DDDDK-tag antibody MBL International Cat# M185-3
I expected that the param being passed by reference to have the same reactivity of the variable being created in the script tag.
Kit_wikicite
nach der ein Schwangerschaftsabbruch (SSA) bis zur 12. Woche nach dem 1. Tag der
Sicher? Ich dachte 14 Wochen ab menstruation und 12 ab Empfängnis?
https://www.profamilia.de/themen/schwangerschaftsabbruch.html
Paths are traversed in the order they occur in the search path. By default, this means the files in app/assets take precedence, and will mask corresponding paths in lib and vendor.
Doing so also means adding empty import statements to guarantee correct order of evaluation of modules (in ES modules, evaluation order is determined statically by the order of import declarations, whereas in CommonJS – and environments that simulate CommonJS by shipping a module loader, i.e. Browserify and Webpack – evaluation order is determined at runtime by the order in which require statements are encountered).
Here: dynamic loading (libraries/functions) meaning: at run time
We then made our way to the scanner. After removing all metal objects —including a belt and a stray dry-cleaning tag with a staple
Everythingmetal need yo be removed?
Kit_doaj
Someadolescents also create personal sites because their friends have
Some create their online presence as a communication tool because their friends have it and its the easiest way to reach them, texting can go as far as gifs , voice notes and more but the online precence brings you closer to their online precense as you can tag your friends in funny memes, videos or the coolest trip to plan next , it builds togetherness and interaction without seeing that person face to face but as a means of interaction
In some cases, I could also create a component without any <script> tag at all. So in that way, I could actually bulk up the logic in one place if I could get some help from the #with block.
I'm more inclined towards an {@ tag than a {# tag because the indentation could quickly get out of control
Contrast with: https://hyp.is/U_7sXhGREeumDJvbgTImjQ/github.com/sveltejs/svelte/pull/4601
create catalog manifest and CASE files
In this stage we create + upload the ibm-appconnect-operator.tar.gz archive.
unstashes 'repo', 'operatormanifestinfo' 'bundlemanifestinfo' 'csv' So that we have access to operator, operator-init, and bundle fat manifest digests. Also access to csv and operator.yaml file.
run the scrpt create-operator-archive.sh which in turn runs the create-catalog-manifest.sh script, which in turn does:
Downland cp4i-operator-bundle-tools.tar.gz from Artifactory and extract it jenkins-build-scripts/cp4i-operator-bundle-tools, that's so to use the push-images-to-er.sh script later on.
call the create-manifest-image-from-platform-images.sh script, which in turn creates the appconnect-operator-catalog fat manifest with the tag ${VERSION}-${BUILD_TIMESTAMP} and pushes it up to appconnect artifactory. it also creates the OperatorCatalogDigest file.
returning back to create-catalog-manifest.sh, update the deploy/catalogsource.yaml file with the new appconnect-operator-catalog fat manifest's digest value
calls the script push-images-to-er.sh in order to copy appconnect-operator-catalog fat manifest to staging Entitled Registry. copied across using tag->digests, then copied across digest->tags. then copied across arch-specific-tags->arch-digests (to enable va scanning).
back in create-catalog-manifest.sh script, in staging ER, assign "latest" to the newly uploaded catalog fat manifest, ${VERSION}-${BUILD_TIMESTAMP}->latest
Returning back to create-operator-archive.sh,
feed the stashed goodimages.json to create-resources-yaml.sh script. This in turn generates the resource.yaml file under the "case" folder.
Curl the cp4i-operator-bundle-tools.tar.gz from artifactory and put it in the jenkins-build-scripts folder. This folder will get ignrore a bit later.
Download cp4i-deploy-operator.tar.gz from artifactory and extract it in the stable/ibm-appconnect-bundle/tests folder
copy the airgap.sh and put it in the stable/ibm-appconnect-bundle/operators/ibm-appconnect/scripts/ folder
copy all "PROD" goodimages.json images into staging ER.
update "latest" tag to now point to the new uploaded gooimages.json images in staging ER.
Also copy some "dev" goodimages.json images into staging ER. That's so that developers can requests images get pull from dockerhub, but actually get pulled from staging ER thanks to openshift registry redirect.
copy the dev images above the /appc bit. so dockerhub urls don't have to specify /appc. Also retag to latest.
Create ibm-appconnect-operator.tar.gz archive. but exclude:
--exclude "${APP_NAME}/jenkins-build-scripts"
--exclude "${APP_NAME}/.travis.yml"
--exclude "${APP_NAME}/.git"
back in jenkinsfile, upload this archive to artifactory in the "latest" folder, this will overwrite what is already there.
Update jenkins job description with info about what has been built.
triggers the job - test-and-promote-cp4i-demo-system. but it doesn't wait for it to succeed.
resulting files:
create operator manifest image
runs the create-operator-manifests.sh script:
2.1 pulls down each arch image using ${VERSION}-${BUILD_TIMESTAMP}-${arch} tags
2.2 create docker manifest with tag - ${VERSION}-${BUILD_TIMESTAMP}. And add both entries.
2.3 push up operator manifest to appconnect artifactory
2.4 Create the OperatorImageDigest file
Update the operator.yaml file with the fat manifest digests of both appconnect-operator and init image.
create new stash called operatormanifestinfo. This specifically specifies the 2 new top level digest files and the changes made to operator.yaml (with the same digests)
Tagging
I have found that tagging is really helpful. It might be interesting to see what are common themes.
appreciate your help
I think that a major part of improving the issue of abuse and providing consent is building in notifications so that website owners will at least be aware that their site is being marked up, highlighted, annotated, and commented on in other locations or by other platforms. Then the site owner at least has the knowledge of what's happening and can then be potentially provided with information and tools to allow/disallow such interactions, particularly if they can block individual bad actors, but still support positive additions, thought, and communication. Ideally this blocking wouldn't occur site wide, which many may be tempted to do now as a knee-jerk reaction to recent events, but would be fine grained enough to filter out the worst offenders.
Toward the end of notifications to site owners, it would be great if any annotating activity would trigger trackbacks, pingbacks, or the relatively newer and better webmention protocol of the WW3C out of the http://IndieWebCamp.com movement. Then site owners would at least have notifications about what is happening on their site that might otherwise be invisible to them.
Perhaps there's a way to further implement filters or tools (a la Akismet on platforms like WordPress) that allow site users to mark materials as spam, abusive, or other so that they are then potentially moved from "public" facing to "private" so that the original highlighter can still see their notes, but that the platform isn't allowing the person's own website to act as a platform to give reach to bad actors.
Further some site owners might appreciate graded filters (G, PG, PG-13, R, X) so that users or even parents can filter what they're willing to see. Consider also annotations on narrative forms that might be posted as spoilers--how can these be guarded against? (Possibly with CSS and a spoiler tag?) Options can be built into the platform itself as well as allowing server-side options for truly hard cases.
My coding skills are rustier than I wish they were, but I'm available to help/consult if needed.
It is important to note here that the flow does not need to begin with a user interaction. With the rise of asynchronous middleware like redux-saga and redux-observable, the ability to trigger any code on a component anywhere is very useful.
This tag doesn't quite fit: can be used independently (fine-grained/decoupled)
Resulting articles met inclusion criteria for review if they addressed psychiatric side effects of isotretinoin treatment or the neurobehavioral teratology of isotretinoin.
Could I do a search like this where I look up mass articles and make sure that they have the same tag words
acknowledges that high priced textbooks are a barrier to learning because many students do not purchase expensive textbooks
I suspect students also make value judgments--this book is too expensive because that number on the price tag is too high, rather than my financial aid doesn't cover it.
hyperscript is more concise because it's just a function call and doesn't require a closing tag. Using it will greatly simplify your tooling chain.
I suppose this is also an argument that Python tries to make? That other languages have this con:
end or } ?The primary motivation behind virtual-dom is to allow us to write code independent of previous state. So when our application state changes we will generate a new VTree. The diff function creates a set of DOM patches that, based on the difference between the previous VTree and the current VTree, will update the previous DOM tree to match the new VTree.
annotation meta: may need new tag: for: "code independent of previous state."
annotation meta: may need new tag: for: diffs other than source/text code diffs (in this case diffs between virtual DOM trees)
7 blog post data science
Kit_datos_ligados
Kit_semantica
Tag your bestie in the comments!
I wrote this caption so that it tempts people to tag other people. I posted a funny quote about best friends and asked people to “tag their besties” so they can see the post as well and engage with it further. Here’s an example: https://www.instagram.com/p/CGGacUoHq2p/
@quoteoftheday
I also tagged a successful account that wrote in their bio, “Tag @quoteoftheday to be featured on our page!” If they feature my post on their account, it could bring a lot of engagement to my own page. Here’s the account: https://www.instagram.com/quoteoftheday/.
Tag your bestie in the comments!
I wrote this caption so that it tempts people to tag other people. I posted a funny quote about best friends and asked people to “tag their besties” so they can see the post as well and engage with it further. Here’s an example: https://www.instagram.com/p/CGGacUoHq2p/
@quoteoftheday
I also tagged a successful account that wrote in their bio, “Tag @quoteoftheday to be featured on our page!” If they feature my post on their account, it could bring a lot of engagement to my own page. Here’s the account: https://www.instagram.com/quoteoftheday/.
Here, when x is a Boolean value then the section tag acts like an if conditional, but when x is an array then it acts like a foreach loop.
Kit_editoriales
Kit_dimensions
Kit_literatura
fewer faithful supports
(see tag)
Kit_altmetria
Kit_spar
Kit_altmetric
spar/biro/BibliographicCollection
spar/fabio/Ontology
Descripción: la liga corresponde a una etiqueta de Twitter
FACULTAD DE CIENCIAS, UNAM
Layla Michán
Kit_wos
But first, what would motivate any young person today to pull the plug? Well maybe they should consider this for a moment. Who most wants you to stay on the grid? The advertisers. Your boss. Human Resources. The advertisers. Your parents (irony of ironies – once they distrusted it, now they need to tag you electronically, share your Facebook photos and message you to death). The advertisers. The government. Your local authority. Your school. Advertisers.
Going of the grid hurts "The man" in 70's parlance.
How do you manage information flows? If anyone is using a personal wiki-style long term information tool I’d love to hear from you!
I've got a handful of interesting things bookmarked here: https://boffosocko.com/tag/wikis/ which includes a rabbit hole of a request similar to your own.
In short to add wiki-style functionality to my blog, the only functionality that is really needed is that 1) I myself have a edit button on static items, 2) the ability to categorise and tag those items, and 3) keep those items outside of the blog posting stream on the front page, and outside of the RSS feed. WordPress pages fit that description, when I’m logged in, and after adding a plugin to allow categories and tags on pages. So a page based section it is, or rather, will be over time.
I like the idea of this and the overall structure. It reminds me a bit of Wikity which may provide this functionality plus a bit more. I really need to spin up a version and play around with it to see if it will give me what I'm looking for in terms of a blog linked with wiki-like functionality.
It isn't rocket science, but as Jon indicates, it's incredibly powerful.
I use my personal website with several levels of taxonomy for tagging and categorizing a variety of things for later search and research.
Much like the example of the Public Radio International producer, I've created what I call a "faux-cast" because I tag everything I listen to online and save it to my website including the appropriate <audio> link to the.mp3 file so that anyone who wants to follow the feed of my listens can have a playlist of all the podcast and internet-related audio I'm listening to.
A visual version of my "listened to" tags can be found at https://boffosocko.com/kind/listen/ with the RSS feed at https://boffosocko.com/kind/listen/feed/
When I received Chris’s comment, my first response was that I should delete my post or at least the incorrect part of it. It’s embarrassing to have your incorrect understandings available for public view. But I decided to leave the post as is but put in a disclaimer so that others would not be misled by my misunderstandings. This experience reminded me that learning makes us vulnerable. Admitting that you don’t know something is hard and being corrected is even harder. Chris was incredibly gentle in his correction. It makes me think about how I respond to my students’ work. Am I as gentle with their work as Chris was to mine? Could I be more gentle? How often have I graded my students’ work and only focused on what they did wrong? Or forgotten that feeling of vulnerability when you don’t know something, when you put your work out for others to judge? This experience has also reminded me that it’s important that we as teachers regularly put ourselves into situations in which we authentically grapple with not knowing something. We should regularly share our less than fully formed understandings with others for feedback. It helps us remember that even confident learners can struggle with being vulnerable. And we need to keep in mind that many of our students are not confident learners.
I'm reminded here of the broad idea that many bloggers write about sooner or later of their website being a "thought space" or place to contemplate out in the open. More often than not, even if they don't have an audience to interact with, their writings become a way of thinking out loud, clarifying things for themselves, self-evolving, or putting themselves out there for potential public reactions (good, bad, or indifferent).
While writing things out loud to no audience can be helpful and useful on an individual level, it's often even more helpful to have some sort of productive and constructive feedback. While a handful of likes or positive seeming responses can be useful, I always prefer the ones that make me think more broadly, deeply, or force me to consider other pieces I hadn't envisioned before. To me this is the real value of these open and often very public thought spaces.
For those interested in the general idea, I've been bookmarking/tagging things around the idea of thought spaces I've read on my own website. Hopefully this collection helps others better understand the spectrum of these ideas for themselves.
With respect to the vulnerability piece, I'm reminded of an episode of <cite>The Human Current</cite> I listened to a few weeks back. There was an excellent section that touched on building up trust with students or even a class when it comes to providing feedback and criticism. Having a bank of trust makes it easier to give feedback as well as to receive it. Here's a link to the audio portion and a copy of the relevant text.
The Task Annotation Project in Science (TAPS) provides K-12 educators with annotated assessment tasks, aligned to the Next Generation Science Standards, that help guide teachers in more equitably monitoring their students’ learning.37 Osmosis is a repository of open educational resources (OER) created to crowdsource the future of medical education.38 Undergraduate and graduate medical students have access to thousands of digital resources, and they have also used annotation - through comments, feedback forms, and ratings - to improve the quality of these learning materials.39 The National Science Digital Library (NSDL), created in 2000, is an archive of open access teaching and learning resources for learners of all ages across science, technology, engineering, and mathematics disciplines.40 Annotation has been used to tag the NSDL’s resources and improve information accessibility, support student interaction with multimedia content through a digital notebook, and educators have annotated NSDL resources to design online learning activities for their students.41 And research about the digital annotation tool Perusall.d-undefined, .lh-undefined { background-color: rgba(0, 0, 0, 0.2) !important; }.d-undefined, .lh-undefined { background-color: rgba(0, 0, 0, 0.5) !important; }3Troy Hicks, Nate Angell, Jeremy Dean, often used in conjunction with science textbooks, has shown that college students’ pre-reading and annotation practices can subsequently improve exam performance.
ites of heightened, future-oriented public debate aboutpossible futures
tag
ites of heightened, future-oriented public debate aboutpossible futures
tag
批注功能支持 Markdown 语法、LaTeX 公式和添加标签（tag）。
确实厉害
Note: This rebuttal was posted by the corresponding author to Review Commons. Content has not been altered except for formatting.
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Response to Reviewers and Revision Plan
We thank all three reviewers for their time and their comments on our manuscript.
Reviewer #1 (Evidence, reproducibility and clarity (Required)):
Here Ryan et al. have used localization analysis following induced rapid relocalization of endogenous proteins to investigate the composition and recruitment hierarchy of a clathrin-TACC3-based spindle complex that is important for microtubule organization and stability.
The authors generate different HeLa cell lines, each with one of four complex members (TACC3, CLTA, chTOG and GTSE1) endogenously tagged with FKBP-GFP via Cas9-mediated editing. This tag allows rapid recruitment to the mitochondria upon rapamycin addition ("knocksideways"). They ultimately quantify each of the 4 components' localization to the spindle following knocksideways of each component using fluorescently-tagged transfected constructs. The authors' interpretation of the results of this analysis are summarized in the last model figure, in which a core MT-binding complex of clathrin and TACC3 recruit the ancillary components GTSE1 and chTOG. In addition, the authors investigate the contribution of individual clathrin-binding LIDL motifs in GTSE1 to the recruitment of clathrin and GTSE1 to spindles. Their findings here largely agree with and confirm a recent report regarding the contribution of these motifs to GTSE1 recruitment to the spindle. They further analyzed GTSE1 fragments for interphase and mitotic microtubule localization, and identified a second region of GTSE1 required (but not sufficient) for spindle localization. Finally, the authors report that PIK3C2A is not part of this complex, contradicting (correcting) a previously published study.
**Major comments:**
1.The chTOG-FKBP-GFP cell line the authors generate has only a small fraction of chTOG tagged, and thus should not be used for any conclusions about protein localization dependency on chTOG. Because they were unable to construct a HeLa cell line with all copies tagged, the authors expect that the homozygous knock-in of chTOG-FKBP-GFP is lethal, and thus their experience is appropriate to report. However, the authors should not use this cell line alone to make statements about chTOG dependency. They would have to use similar localization analysis, but after another method to disrupt chTOG (as a second-best approach), such as RNAi. In fact, they have reported this in a previous publication (Booth et al 2011). However, the result was different. There, loss of chTOG resulted in reduced clathrin on spindles, suggesting it may stabilize or help recruit the complex. Alternatively, they could remove their chTOG data, but this would compromise the "comprehensive" nature of the work.
The referee is correct. The point here is to show the results we had using this approach for all four proteins under study. For this reason, we do not want to remove this data and prefer to show our results “warts-and-all”. We feel that the shortcomings of our approach are honestly presented and discussed in the manuscript. While only a fraction of chTOG was tagged, we should expect some co-removal after its induced mislocalization. Since we saw no change, we concluded that chTOG is auxiliary.
The “second best” approach suggested (RNAi of chTOG) is problematic for two reasons. First, chTOG RNAi results in gross changes to spindle structure (multipolar spindles) and it is difficult to pick apart differences in protein partner localization that result from loss of chTOG from those resulting from changes in spindle structure. Second, the paper is about induced mislocalization as a method for determining protein complexes once a normal spindle has formed. So, removing chTOG prior to mitosis is not comparable. If we get the same or different result, does it confirm or conflict with the data we have? Nonetheless, given the discrepancy with our earlier work, we should investigate this further.
To address this concern, we will stain endogenous clathrin, TACC3 and GTSE1 following chTOG RNAi and measure their relative levels at the spindle.
Making the chTOG-FKBP-GFP cell line was difficult. As described in the paper, we only recovered heterozygous clones despite repeated attempts. Since submission, we have been made aware of a HCT116 chTOG-FKBP-GFP cell line that is reported to be homozygously tagged (Cherry et al. 2019 doi: 10.1002/glia.23628).
A note about this cell line has been added to the paper (Results section, final sentence of 1st paragraph).
2.The authors initially analyze complex member localization after knocksideways experiments by antibody staining, which has the advantage of analyzing endogenous proteins (versus the later transfected fluorescent constructs). Setting aside potential artefacts from fixation, this would seem to be a better method for controlled analysis to take advantage of their setup (short of generating stable cell lines with second proteins endogenously tagged in a second color - a huge undertaking). The authors conclude that antibody specificity problems confounded their analysis and explained unusual results. However, I think is worth investing a little more effort to sort this out, rather than bringing doubt to the whole data set. Verifying and then using another antibody for chTOG localization would be informative. Of course, the negative control should not be their chTOG-FKBP-GFP line, as it does not relocalize most of chTOG.
In the case of GTSE1, an alternative explanation to antibody specificity issues would be that the GTSE1-FKBP-GFP cell line is not in fact homozygously tagged. Given the low expression levels on the western provided, and the detection of GTSE1 on the spindle in the induced GTSE1-FKBP-GFP cell line (but not TACC3-FKBP-GFP), it seems plausible that an untagged copy remains. If there are multiple copies of GTSE1 in Hela cells, one untagged copy could represent a small fraction of total GTSE1. This should thus be ruled out. GTSE1 clones should be analyzed with more protein extracts loaded - dilutions of the extracts can determine the sensitivity of the blot to lower protein levels. In addition, sequencing of genomic DNA can reveal a small percentage with different reads.
We used a two-pronged approach for assessing relocalization of protein partners (staining vs transfected constructs). The staining approach is superior since endogenous proteins are examined, but it is limited by antibody specificity. The transfection approach overcomes this limitation but is in turn limited by effects of overexpression and tagging. Together the two approaches allow us, and anyone employing this method, to get a picture of protein complexes. We didn’t want to create the impression that one or other approach is confounded, but the referee is correct that this analysis would benefit from further work.
Specifically, to address these concerns:
3.There is a lot of data contained in the small graphs summarizing quantification of localization in Figs 3 and 4. They would be more accessible to the reader if they were larger and/or an "example" of the chart with labels was present explaining it (essentially what is in the figure legends). Furthermore, there is no statistical test applied to this data that I see. This is needed. How do authors determine whether there is an "effect"?
Our aim was to compress a lot of information into a small space, while still showing some example primary data. All reviewers raised the same concern which tells us that we went too far towards “data visualization”.
To address this point, we will rework these figures.
**Minor issues:**
1.The GTSE1 constructs used for mutation and localization analysis are 720 amino acids long. A recent study analyzing similar mutations uses a 739 amino acid construct (Rondelet et al 2020). The latter is the predominant transcript in NCBI and Ensembl databases. It appears the construct used by the authors omits the first 19 a.a.. I do not think using the truncated transcript affects conclusions of the manuscript, but it could generate confusion when identifying residues based on a.a.#s of mutant constructs (Fig 6). This should be somehow clarified.
We were aware of the longer transcript but were using the 720 residue form since it is the canonical sequence in Uniprot (https://www.uniprot.org/uniprot/Q9NYZ3). We did not know that the 739 form is the predominant transcript. We agree this is unlikely to affect our work but that the numbering may cause confusion.
We have added a note to the Methods (Molecular Biology section) to accurately describe what we and Rondelet et al. have used.
2.The labeling of constructs in Fig 6C/D is confusing, and appears shifted by eye at places. Please relabel this more clearly.
Apologies for the error.
We have relabeled Figure 6C,D and also made a similar alteration to Figure 5C.
The recommended new experimental data (Analysis complex member levels on spindles after full perturbation of spindle chTOG; new chTOG antibody stainings in the FKBP lines; reanalysis of GTSE1 DNA/protein in GTSE1-FKBP line) should only require a new antibody/siRNA, plus a few weeks time to repeat the analyses already in the paper with new reagents.
Reviewer #1 (Significance (Required)):
While multiple individual components of this complex have been previously characterized, the structure and nature of the complex formation and its recruitment to microtubules/spindles remains a complex problem that has yet to be solved.
Overall this study represents a comprehensive localization-dependency analysis of the Clathrin-TACC3 based spindle complex using a consistent methodology. Although several of the conclusions of the findings echo previous reports, some of the previous literature is contradictory within itself as well as with the conclusions here. Analyzing all components with a single, rapid-perturbation technique thus has great value to present a clear data set, given that the experimental setup conditions and analysis are solid (a goal to which the majority of comments refer).
Beyond the complex localization/recruitment analysis, two novel findings of this study that emerge are:
a)GTSE1 contains a second, separate protein region, distinct from the clathrin-binding motifs that is required for its localization to the spindle, and most likely a microtubule-interaction site. This suggests that GTSE1 recruitment to the spindle is more complex than previously reported.
b)PI3KC2A, which has been reported previously to be a stabilizing member of this complex, is in fact not a member, nor localizes to spindles, nor displays a mitotic defect after loss. This is important conclusion to be made as it would correct the literature, and avoid future confusion.
--
Reviewer #2 (Evidence, reproducibility and clarity (Required)):
In this paper, the authors investigate the nature of interactions between members of the TACC3-chTOG-clathrin-GTSE1 complex on the mitotic spindle. By using a series of HeLa cell lines that they have created by CRISPR/Cas9 editing to enable spatial manipulation (knocksideways) of either TACC3, chTOG, clathrin and GTSE1, they show that on spindle microtubules TACC3 and clathrin represent core complex members whereas chTOG and GTSE1 bind to them respectively but not to each other. Additionally, the authors find that the protein PIK3C2A, which has been implicated in this complex previously is in fact not a component of this complex in mitotic cells. The main advance of the paper in my opinion is the endogenous tagging of the proteins for knocksideways experiments since former experiments depended on RNAi silencing and expression of tagged proteins from plasmids, which introduced issues of protein silencing efficiency and plasmid overexpression problems. This approach seems to alleviate these problems, except in the case of chTOG which seems to be lethal in its homozygous variant.
**Major comments:**
I find the key conclusions regarding the localization of the components of the complex convincing. There are some issues regarding the specificity of antibodies in immunostaining experiments (Fig 3.) and the influence of mCherry-TACC3 expression on distorted localization of the complex prior to knocksideways. However, I think the general conclusion about which complex components (clathrin and TACC3) influence the localization of the other proteins in the complex (chTOG and GTSE1) stands. One thing that I miss from the paper is the data on the consequences on the spindle shape and morphology after knocksideways. I have noticed on images in both Figure 3 and Figure 4 that in some cases distribution of the signal seems to influence quite a bit the spindle morphology. Also, In Figure 3 I have noticed what seems to me a quite big variation in spindle size in tubulin signal in both untreated and rapamycin cells. Since authors have many of these images already, I believe it would be realistic, not costly and of additional value for the paper to provide more data on the consequences of the knocksideways experiments. Change of spindle size, tubulin intensity and DNA/kinetochore misalignment upon knocksideways would be helpful to appreciate more the findings of the paper. More so since the authors on more than one occasion find their motivation in the field of cancer research and spindle stability relation to it. Some data connection to this motivation would be of value. Experiments seem reproducible.
The focus of the paper is on using the knocksideways methodology to understand a protein complex during mitosis, rather than looking at its function. We are not keen to do new experiments that are not part of the central message of the paper. However, the Reviewer is correct that we do already have a dataset that can be mined in the manner described.
To address this point, we will analyze spindle size parameters and also the intensity of tubulin. Our analysis will be limited to the short timeframe of our experiments, but it should reveal or refute any changes in spindle structure that may result from loss of complex members.
**Minor comments:**
I have some problems with the clarity of Figure 3 and 4. For Figure 3. In Figure 3 plots on the right are a bit small and not easy to read. Some reorganization of the figure might be beneficial. In Figure 4 plots to the right are also too small to be clear. Also, I miss the number of cells (n) I can't see the number of individual arrows because of the size of graphs.
Our aim was to compress a lot of information into a small space, while still showing some example primary data. All reviewers raised the same concern which tells us that we went too far towards “data visualization”.
To address this point, we will rework these figures.
Reviewer #2 (Significance (Required)):
I find that the biggest significance of the paper is in the creation of new tools (cell lines) to study the localization of proteins TACC3, chTOG, clathrin and GTSE1. Cell lines where endogenous proteins can be delocalized rapidly will be of value for scientist working not only in mitosis but such as in the case of clathrin research, vesicle formation and trafficking or p53-dependent apoptosis in the case of GTSE1. In the field of mitosis it will surely help and speed up the research concerning the role of these proteins in spindle assembly and stability.
Field of expertise: mitotic spindle
--
Reviewer #3 (Evidence, reproducibility and clarity (Required)):
**Summary:**
This papers analyses the chTog/TACC3/clathrin/GTSE1 complex that crosslinks and stabilises microtubule bundles in the mitotic spindle. The authors have developed an elegant knock sideways approach to specifically analyse the effects of removing individual components of the complex from the spindle and study the effect this has on the other interactors. They report, based on these assays that the core of the complex is formed by TACC3 and Clathrin while GTSE1 and chTog are auxiliary interactors. They also refute previous evidence that this complex also incorporates PIK3C2A. Overall, this is an interesting study that distinguishes itself predominantly by its methodology. However, some of the reported results need more thorough analysis to allow convincing conclusions.
**Major comments:**
1)The knockside way method is the main highlight if this paper. Unlike previous studies by the PI, this time endogenous genes are tagged which is a key advance and allows much better interpretation of the results. I am not sure why the authors have chosen HeLa cells as their model here, given the messed up genome of these cells. A non-transformed cell line would have been preferable, but as a proof of principle study, I think HeLa are acceptable, and I wouldn't expect the authors to repeat all the experiment in another system.
Figure 1,2 and S1 are describing and validating this approach in some detail, but this will require some more work.
The authors state that gene targeting was validated using a combination of PCR, sequencing, Western blotting, but show only the results for westerns. PCR analysis that demonstrates homozygous or heterozygous gene targeting should be shown here.
Another issue is the penetrance of the phenotypes induced by Rapamycin. The authors show nice data of the system working in individual cells but do not give us an idea if this happens in all cells. The localisation of the individual tagged genes should be quantified (ideally with line plots) in 50 randomly chosen mitotic cells with 3 repeats before and after rapamycin treatment. Moreover, the analysis of mitotic duration (Figure S1D) should be extended to include a plus Rapamycin cohort and this should be moved in the main Figure.
If the system works only in a small proportion of cells, this should be clearly stated. I don't think this would prevent publication, but it is an important piece of information that is missing.
The Reviewer raises two issues here.
2)Apart from a simple quantification of mitotic duration, I believe a more detailed mitotic phenotype analysis for each knock-side way gene, especially the homozygous targeted clones, should be included. This can involve more high-resolution live cell imaging of mitotic progression with SiR-DNA and GFP-tubulin, using the dark mitotrap.
We don’t agree that such an analysis should be included. The focus of this paper is on using the knocksideways methodology to understand a protein complex during mitosis, and not looking at its function. There are several papers on the mitotic phenotypes of these genes probed using RNAi in different cellular systems (examples for chTOG: 10.1101/gad.245603; TACC3/clathrin: 10.1038/emboj.2011.15, 10.1242/jcs.075911, 10.1083/jcb.200911091, 10.1083/jcb.200911120; GTSE1: 10.1083/jcb.201606081). Moreover, our 2013 paper used knocksideways (with RNAi and overexpression) and has a detailed analysis of mitotic progression, microtubule stability, checkpoint activity and kinetochore motions (Cheeseman et al., 2013 doi: 10.1242/jcs.124834).
New experiments that are not part of the central message of the paper and are unlikely to give new insight are not the best use of our revision efforts for this paper (especially during the pandemic). Having said this, Reviewer 2’s suggestion to use our existing dataset to investigate mitotic phenotypes, will largely answer Reviewer 3’s request.
We will analyze spindle size parameters and also the intensity of tubulin. Our analysis will be limited to the short timeframe of our experiments, but it should reveal or refute any changes in spindle structure that result from the loss of complex members.
3)Overall, the quantitative analysis in Figure 3 ,4 and 7 is not good enough and sometimes doesn't fully support the conclusions. In Figure 3,4 a convoluted way of demonstrating the change in localisation is shown and this panel is so small that is almost impossible to read. Also, there is no statistical analysis, and the sample size seems very small . At least 25 cells should be analysed here in 3 repeats. I would suggest to unify the quantification in the MS and use the line plots shown in Figure 5 and 6 and compare each protein before and after rapamycin addition. This is much easier to read and more convincing. The images of the cells panels can be moved to a supplement as they contain very little information. This would generate space to expand the size and depth of the quantitative analysis. Instead of Anova tests, I would recommend using a simple t-test comparing each condition to its relevant control since this is the only relevant comparison in the experiment. Statistical significance should be calculated for each experiment with sufficient sample size. It would also be better to show the individual data points from the three repeats in different colours so that the reproducibility between repeat can be judged.
This type of statistical analysis should be uniformly done throughout the MS and also extended to Figure 7.
The referee raises several issues here with our data presentation and statistical analysis.
Reviewer #3 (Significance (Required)):
In my opinion, the most interesting aspect of the MS is the methodology. Based on this, publication is justified and will be of interest to a wider audience. That is why a more detailed analysis of the penetrance of this manipulation across the cell population will be critical.
The application of this method to analyse the composition of the TACC3/Clathrin complex on the spindle is the main biological advance, and the novel information is rather limited but not unimportant.
Overall, if these results can be properly quantified I would recommend publication.
Note: This preprint has been reviewed by subject experts for Review Commons. Content has not been altered except for formatting.
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Here Ryan et al. have used localization analysis following induced rapid relocalization of endogenous proteins to investigate the composition and recruitment hierarchy of a clathrin-TACC3-based spindle complex that is important for microtubule organization and stability. The authors generate different HeLa cell lines, each with one of four complex members (TACC3, CLTA, chTOG and GTSE1) endogenously tagged with FKBP-GFP via Cas9-mediated editing. This tag allows rapid recruitment to the mitochondria upon rapamycin addition ("knocksideways"). They ultimately quantify each of the 4 components' localization to the spindle following knocksideways of each component using fluorescently-tagged transfected constructs. The authors' interpretation of the results of this analysis are summarized in the last model figure, in which a core MT-binding complex of clathrin and TACC3 recruit the ancillary components GTSE1 and chTOG. In addition, the authors investigate the contribution of individual clathrin-binding LIDL motifs in GTSE1 to the recruitment of clathrin and GTSE1 to spindles. Their findings here largely agree with and confirm a recent report regarding the contribution of these motifs to GTSE1 recruitment to the spindle. They further analyzed GTSE1 fragments for interphase and mitotic microtubule localization, and identified a second region of GTSE1 required (but not sufficient) for spindle localization. Finally, the authors report that PIK3C2A is not part of this complex, contradicting (correcting) a previously published study.
Major comments:
1.The chTOG-FKBP-GFP cell line the authors generate has only a small fraction of chTOG tagged, and thus should not be used for any conclusions about protein localization dependency on chTOG. Because they were unable to construct a HeLa cell line with all copies tagged, the authors expect that the homozygous knock-in of chTOG-FKBP-GFP is lethal, and thus their experience is appropriate to report. However, the authors should not use this cell line alone to make statements about chTOG dependency. They would have to use similar localization analysis, but after another method to disrupt chTOG (as a second-best approach), such as RNAi. In fact, they have reported this in a previous publication (Booth et al 2011). However, the result was different. There, loss of chTOG resulted in reduced clathrin on spindles, suggesting it may stabilize or help recruit the complex. Alternatively, they could remove their chTOG data, but this would compromise the "comprehensive" nature of the work.
2.The authors initially analyze complex member localization after knocksideways experiments by antibody staining, which has the advantage of analyzing endogenous proteins (versus the later transfected fluorescent constructs). Setting aside potential artefacts from fixation, this would seem to be a better method for controlled analysis to take advantage of their setup (short of generating stable cell lines with second proteins endogenously tagged in a second color - a huge undertaking). The authors conclude that antibody specificity problems confounded their analysis and explained unusual results. However, I think is worth investing a little more effort to sort this out, rather than bringing doubt to the whole data set. Verifying and then using another antibody for chTOG localization would be informative. Of course, the negative control should not be their chTOG-FKBP-GFP line, as it does not relocalize most of chTOG.
In the case of GTSE1, an alternative explanation to antibody specificity issues would be that the GTSE1-FKBP-GFP cell line is not in fact homozygously tagged. Given the low expression levels on the western provided, and the detection of GTSE1 on the spindle in the induced GTSE1-FKBP-GFP cell line (but not TACC3-FKBP-GFP), it seems plausible that an untagged copy remains. If there are multiple copies of GTSE1 in Hela cells, one untagged copy could represent a small fraction of total GTSE1. This should thus be ruled out. GTSE1 clones should be analyzed with more protein extracts loaded - dilutions of the extracts can determine the sensitivity of the blot to lower protein levels. In addition, sequencing of genomic DNA can reveal a small percentage with different reads.
3.There is a lot of data contained in the small graphs summarizing quantification of localization in Figs 3 and 4. They would be more accessible to the reader if they were larger and/or an "example" of the chart with labels was present explaining it (essentially what is in the figure legends). Furthermore, there is no statistical test applied to this data that I see. This is needed. How do authors determine whether there is an "effect"?
Minor issues:
1.The GTSE1 constructs used for mutation and localization analysis are 720 amino acids long. A recent study analyzing similar mutations uses a 739 amino acid construct (Rondelet et al 2020). The latter is the predominant transcript in NCBI and Ensembl databases. It appears the construct used by the authors omits the first 19 a.a.. I do not think using the truncated transcript affects conclusions of the manuscript, but it could generate confusion when identifying residues based on a.a.#s of mutant constructs (Fig 6). This should be somehow clarified.
2.The labeling of constructs in Fig 6C/D is confusing, and appears shifted by eye at places. Please relabel this more clearly.
The recommended new experimental data (Analysis complex member levels on spindles after full perturbation of spindle chTOG; new chTOG antibody stainings in the FKBP lines; reanalysis of GTSE1 DNA/protein in GTSE1-FKBP line) should only require a new antibody/siRNA, plus a few weeks time to repeat the analyses already in the paper with new reagents.
While multiple individual components of this complex have been previously characterized, the structure and nature of the complex formation and its recruitment to microtubules/spindles remains a complex problem that has yet to be solved.
Overall this study represents a comprehensive localization-dependency analysis of the Clathrin-TACC3 based spindle complex using a consistent methodology. Although several of the conclusions of the findings echo previous reports, some of the previous literature is contradictory within itself as well as with the conclusions here. Analyzing all components with a single, rapid-perturbation technique thus has great value to present a clear data set, given that the experimental setup conditions and analysis are solid (a goal to which the majority of comments refer).
Beyond the complex localization/recruitment analysis, two novel findings of this study that emerge are:
a)GTSE1 contains a second, separate protein region, distinct from the clathrin-binding motifs that is required for its localization to the spindle, and most likely a microtubule-interaction site. This suggests that GTSE1 recruitment to the spindle is more complex than previously reported.
b)PI3KC2A, which has been reported previously to be a stabilizing member of this complex, is in fact not a member, nor localizes to spindles, nor displays a mitotic defect after loss. This is important conclusion to be made as it would correct the literature, and avoid future confusion.
that
that's what.
The general justification for appropriating the tag has been that, in addition to killing Black people, White supremacy also continues to kill and harm a lot of non-Black people of color as well.
This year we have really highlighted the tragic deaths of many black people. We call people out for their racist behaviors and views. We are getting closer to uncovering the corruption some people have and cancelling them for having them. In this case I feel cancel culture would be legitimate because of how these people are looking down upon groups of people.
Congress appears to have missed a key point in its questioning last week. It’s clear that fake news and outright lies are, in fact, a small portion of the total content on any of the big tech platforms. But what matters are the routes that these companies provide to unreliable sources of information. You don’t have to silence Julian Assange or some random Twitter account that’s set up to look like a real news outfit, but you also don’t have to inject them into a legitimate news discussion.
For something to pop up on the top "news" section, I think these developers should have to fact check and read through the information. They could also add a tag such as potentially untruthful which would help stop spread the misinformation..
Why Are Finland’s Schools Successful? The country’s achievements in education have other nations, especially the United States, doing their homework <img src="https://thumbs-prod.si-cdn.com/thzZYTv2Evhq3x8iHdcaakihfVE=/800x600/filters:no_upscale()/https://public-media.si-cdn.com/filer/cd/ee/cdee1c82-f8e3-4de4-983e-8599d4485745/finland-smiles-wr.jpg" alt="Kirkkojarvi School" itemprop="image"> "This is what we do every day," says Kirkkojarvi Comprehensive School principal Kari Louhivuori, "prepare kids for life." (Stuart Conway) By LynNell Hancock Smithsonian Magazine | Subscribe September 2011 AddThis Sharing ButtonsShare to FacebookFacebookShare to TwitterTwitterShare to RedditReddit78Share to PinterestPinterest997Share to LinkedInLinkedInShare to FlipboardFlipboardShare to EmailEmailShare to PrintPrintShare to MoreAddThis934 It was the end of term at Kirkkojarvi Comprehensive School in Espoo, a sprawling suburb west of Helsinki, when Kari Louhivuori, a veteran teacher and the school’s principal, decided to try something extreme—by Finnish standards. One of his sixth-grade students, a Kosovo-Albanian boy, had drifted far off the learning grid, resisting his teacher’s best efforts. The school’s team of special educators—including a social worker, a nurse and a psychologist—convinced Louhivuori that laziness was not to blame. 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n=r.generatePrerollTag(e,t);r.monetization.onPrerollAdOpportunity(n)}),f()(this,"onSeekedWhileAdInProgress",function(){r.monetization.onMidrollAdOpportunity()});var i=t.getState;this.monetization=n,this.videoTimeSubscriber=new qi(t,this),this.videoSeekSubscriber=new zi(t,this),this.prerollScheduler=new Gi(t,this);var o=_i.adTagUrlTemplate(i());this.adTagGenerator=new Wi(o)},Yi=function(){function e(){Ai()(this,e)}return Vi()(e,null,[{key:"generateAdRequest",value:function(e,t,n){var r=new google.ima.AdsRequest;return r.adTagUrl=e,Fn()||r.setAdWillPlayMuted(t),r.vastLoadTimeout=n,r}}]),e}(),Zi=function(e){return function(t){t({type:"[MONETIZATION] change ad status",payload:e})}},Xi=function(e){return function(t){t({type:"[COMMON] set pending video status",payload:{pendingStatusObject:{type:e,value:""}}})}},Ji=function(e){return function(t){t({type:"[MONETIZATION] change loading ad status",payload:e})}},Qi=function(e){return function(t){t({type:"[MONETIZATION] update ad 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t=a.store,n=t.getState,r=t.dispatch,i=gn.volume(n());Bn()||gn.muted(n())?(e.setVolume(0),Qi(!0)(r)):(e.setVolume(gn.volume(n())),eo(i)(r),Qi(!1)(r))}),f()(this,"createIMAAdManager",function(t){a.IMAAdManager=t.getAdsManager(a.adVideoElement,e.getAdsRenderingSettings()),a.setAdVolume(a.IMAAdManager)}),f()(this,"registerToAdManagerEvents",function(){a.IMAAdManager.addEventListener(google.ima.AdErrorEvent.Type.AD_ERROR,a.onAdError),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.CONTENT_PAUSE_REQUESTED,a.onContentPauseRequested),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.CONTENT_RESUME_REQUESTED,a.onContentResumeRequested),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.STARTED,a.onAdStarted),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.IMPRESSION,a.onAdImpression),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.SKIPPED,a.onAdSkipped),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.COMPLETE,a.onAdCompleted),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.PAUSED,a.onAdPaused),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.RESUMED,a.onAdStarted),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.AD_PROGRESS,a.onAdProgressChanged),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.VOLUME_CHANGED,a.onVolumeChanged),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.VOLUME_MUTED,a.onAdVolumeMutedChanged),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.ALL_ADS_COMPLETED,a.onAdCompleted)}),f()(this,"onIMAAdsManagerLoaded",function(e){var t=a.store.dispatch;a.createIMAAdManager(e),a.registerToAdManagerEvents(),Zi("loaded")(t)}),f()(this,"onAdError",function(e){var t=a.store.dispatch;!function(e){return function(t){t({type:"[MONETIZATION] change ad error",payload:e})}}(e.getError().getMessage())(t),Ji(!1),a.continuePlayingContent()}),f()(this,"onAdImpression",function(e){var t=a.store.dispatch,n=!e.getAd().g.vpaid;a.setPodInfo(e),function(e){e({type:"[MONETIZATION] increase ad impression counter"})}(t),function(e){return function(t){t({type:"[MONETIZATION] update is vast ad",payload:e})}}(n)(t)}),f()(this,"onVolumeChanged",function(e){var t=a.store.dispatch;eo(e.target.getVolume())(t)}),f()(this,"onAdVolumeMutedChanged",function(e){var t=a.store.dispatch;0===e.target.getVolume()?Qi(!0)(t):Qi(!1)(t)}),f()(this,"continuePlayingContent",function(){var e=a.store,t=e.getState,n=e.dispatch,r=hn.videoTagStatus(t());Xi("idle"===r?"play":"resume")(n)}),f()(this,"stopPlayingContent",function(){var 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e=a.store.dispatch;Zi("skipped")(e)}),f()(this,"onResize",function(){Un(a.IMAAdManager)||(a.IMAAdManager.resize(a.videoPlayerElement.clientWidth,a.videoPlayerElement.clientHeight,google.ima.ViewMode.NORMAL),a.adContainerElement.style.height="".concat(a.videoPlayerElement.clientHeight,"px"))}),f()(this,"onAdProgressChanged",function(e){var t,n,r=a.store,i=r.dispatch,o=r.getState,s=e.getAdData().currentTime,u=e.getAdData().duration,c=_i.adDuration(o());(t=s,function(e){e({type:"[MONETIZATION] change ad current time",payload:t})})(i),c!==u&&(n=u,function(e){e({type:"[MONETIZATION] change ad duration",payload:n})})(i)}),f()(this,"onAnchorStatusChanged",function(){var e=a.store.getState;"processing"!==Pr(e())&&a.onResize()}),f()(this,"changeAdVolume",function(e){Un(a.IMAAdManager)||a.IMAAdManager.setVolume(e)}),f()(this,"changeAdMuted",function(e,t){Un(a.IMAAdManager)||(t?a.IMAAdManager.setVolume(0):a.IMAAdManager.setVolume(e))}),f()(this,"changeAdStatus",function(e){Un(a.IMAAdManager)||("playing"===e&&a.IMAAdManager.resume(),"paused"===e&&a.IMAAdManager.pause())});var s=t.getState;this.store=t,this.adVideoElement=r,this.videoPlayerElement=i,this.adContainerElement=n,this.adDisplayContainer=new google.ima.AdDisplayContainer(n,r),this.createAdLoader(s(),this.adDisplayContainer),this.adDisplayContainer.initialize(),this.anchorStatusStoreSubscriber=new ji(t,e.getAnchorDependencies,this.onAnchorStatusChanged.bind(this)),this.registerForWindowResize(),this.initMutationObserver(o)};f()(to,"getAdsRenderingSettings",function(){var e=new google.ima.AdsRenderingSettings;return 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e=s.store,t=e.dispatch,n=e.getState,r=_i.adStatus(n()),i=bi.continuePlayingWhileWaitingForAd(n());"loaded"===r?s.playAd(!0):"requested"===r&&(s.pendingMidrollAdPlay=!0,i||(Xi("pause")(t),Ji(!0)(t))),function(e){e({type:"[MONETIZATION] increase ad Opportunity counter"})}(t)}),f()(this,"onPrerollAdOpportunity",function(e){var t=s.store,n=t.getState,r=t.dispatch,i=Fi.loadingImaStatus(n());Un(s.adHandler)?"loading"!==i&&""!==i||(Ji(!0)(r),s.pendingPrerollAdPlay=!0,s.pendingPrerollAdTag=e):(s.pendingPrerollAdPlay=!0,Ji(!0)(r),s.adHandler.loadNewAd(e,"preroll"))}),f()(this,"onPreMidrollAdOpportunity",function(e,t){Un(s.adHandler)||(e.currentTime>=e.midrollTime&&(s.pendingMidrollAdPlay=!0),s.pendingMidrollNumber=e.midrollNumber,s.adHandler.loadNewAd(t,"midroll"))}),f()(this,"hasPendingAd",function(){return s.hasPendingMidrollAdPlay()||s.hasPendingPrerollAdPlay()}),f()(this,"onAdStatusChanged",function(e){var t=s.store.dispatch,n=_i.adStatus(e);"completed"===n&&Ji(!1)(t);var r=bi.continuePlayingWhileWaitingForAd(e),i=_i.loadingAd(e);"playing"!==n&&"error"!==n||r||!i||Ji(!1)(t),s.hasPendingAd()&&"loaded"===n?s.playAd(s.hasPendingMidrollAdPlay()):s.hasPendingAd()&&"error"===n?(Ji(!1),s.clearPendingMidroll(),s.clearPendingPreroll()):Hi(n)||(Ji(!1),function(e){e({type:"[MONETIZATION] clear ad data"})}(t))}),f()(this,"clearPendingMidroll",function(){s.pendingMidrollNumber=null,s.pendingMidrollAdPlay=!1}),f()(this,"clearPendingPreroll",function(){s.pendingPrerollAdPlay=!1,s.pendingPrerollAdTag=null}),f()(this,"onVideoTagStatusChanged",function(e){"complete"===hn.videoTagStatus(e)&&function(e){e({type:"[MONETIZATION] clear played midrolls"})}(s.store.dispatch)}),f()(this,"hasPendingMidrollAdPlay",function(){return s.pendingMidrollAdPlay}),f()(this,"hasPendingPrerollAdPlay",function(){return s.pendingPrerollAdPlay}),f()(this,"playAd",function(e){var t,n=s.store.dispatch,r=s.adHandler.playAd();e?((t=s.pendingMidrollNumber,function(e){e({type:"[MONETIZATION] add 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Ki(t,this),this.adStatusSubscriber=new ji(t,e.getAdStatusDependencies,this.onAdStatusChanged.bind(this)),this.videoTagStatusSubscriber=new ji(t,e.getVideoTagStatusDependencies,this.onVideoTagStatusChanged.bind(this)),e.canUseIMA(u())?this.adHandler=new to(t,r,i,o,a):this.imaLoadingStatusSubscriber=new ji(t,e.getIMALoadingStatusDependencies,this.onIMALoadingStatusChanged.bind(this)),this.pendingAdStatusStoreSubscriber=new ji(t,e.getPendingAdStatusDependencies,this.onPendingAdStatusChanged.bind(this)),this.adMutedStoreSubscriber=new ji(t,e.getAdMutedDependencies,this.onAdMutedChanged.bind(this)),this.adVolumeStoreSubscriber=new ji(t,e.getAdVolumeDependencies,this.onAdVolumeChanged.bind(this))};f()(no,"getAdStatusDependencies",function(e){return[_i.adStatus(e)]}),f()(no,"getVideoTagStatusDependencies",function(e){return[hn.videoTagStatus(e)]}),f()(no,"getIMALoadingStatusDependencies",function(e){return[Fi.loadingImaStatus(e)]}),f()(no,"canUseIMA",function(e){return"success"===Fi.loadingImaStatus(e)}),f()(no,"getPendingAdStatusDependencies",function(e){return[_i.pendingAdStatus(e)]}),f()(no,"getAdMutedDependencies",function(e){return[_i.adMuted(e)]}),f()(no,"getAdVolumeDependencies",function(e){return[_i.adVolume(e)]});var ro=function(e,t){!function(e,t){var n=document.getElementById(vn(t));B(b(Li,{store:e,playerId:t}),n)}(e,t);var n=function(e){var t=Ri(e);return document.getElementById(t)}(t),r=function(e){var t=Bn()?Di(e):En(e);return document.getElementById(t)}(t),i=function(e){var t=En(e);return document.getElementById(t)}(t),o=function(e){var t=bn(e);return document.getElementById(t)}(t);return new 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this.errorMessage=e,this}},{key:"setAdPodNumber",value:function(e){return this.adPodNumber=e,this}},{key:"setAdSlotNumber",value:function(e){return this.adSlotNumber=e,this}},{key:"build",value:function(){var e=[];return jn(this.position)||e.push("video current position=".concat(Hn(this.position),"sec")),jn(this.duration)||e.push("video duration time=".concat(Hn(this.duration),"sec")),jn(this.loadTime)||e.push("video load time=".concat(this.loadTime,"milliseconds")),jn(this.previousPosition)||e.push("previous position=".concat(Hn(this.previousPosition),"sec")),jn(this.adOrder)||e.push("ad order=".concat(this.adOrder)),jn(this.adType)||e.push("ad type=".concat(this.adType)),jn(this.adDuration)||e.push("ad duration=".concat(Hn(Number(this.adDuration)),"sec")),jn(this.adPodNumber)||e.push("pod number=".concat(this.adPodNumber)),jn(this.adSlotNumber)||e.push("slot number=".concat(this.adSlotNumber)),jn(this.errorMessage)||e.push("error 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The initial state may not be undefined, but can be null.')})}(n)}catch(s){o=s}return function(e,t){if(void 0===e&&(e={}),o)throw o;for(var r=!1,i={},s=0;s<a.length;s++){var u=a[s],c=n[u],l=e[u],d=c(l,t);if("undefined"===typeof d){var p=mt(u,t);throw new Error(p)}i[u]=d,r=r||d!==l}return(r=r||a.length!==Object.keys(e).length)?i:e}}({dependenciesLoadingStatus:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:da,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] update hls status":return la(la({},e),{},{loadingHLSStatus:t.payload});case"[CORE] update ima status":return la(la({},e),{},{loadingImaStatus:t.payload});default:return e}},playerData:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:ha,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":var n=t.payload;return fa({},function(e,t,n){var r=t.playback_method,i=t.player_id;return fa(fa({},e),{},{playbackMethod:Un(r)?e.playbackMethod:r,playerId:Un(i)?e.playerId:i,playerInstanceUniqId:n,playerMode:Fn()?"mobile":"desktop"})}(e,n.initiateParams,n.playerInstanceUniqId));case"[CORE] reset player data time params":return fa(fa({},e),{},{currentVideoTimeFragment:0,currentVideoBufferedTime:0,currentVideoDuration:0,currentVideoTime:0});case"[COMMON] set mute video":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{muted:t.payload})});case"[COMMON] set volume":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{volume:t.payload})});case"[COMMON] change selected settings category":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{selectedSettingsCategory:t.payload})});case"[COMMON] change settings speed":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{speed:t.payload})});case"[COMMON] change settings quality":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{quality:t.payload})});case"[COMMON] set fullscreen":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{fullscreen:fa(fa({},e.playerSettings.fullscreen),{},{isFullscreenOn:t.payload,pendingFullscreenRequest:""})})});case"[COMMON] set fullscreen request":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{fullscreen:fa(fa({},e.playerSettings.fullscreen),{},{pendingFullscreenRequest:t.payload})})});case"[COMMON] set pending video status":var r=t.payload.pendingStatusObject;return fa(fa({},e),{},{pendingVideoTagStatus:fa({},r)});case"[COMMON] set player mode":return fa(fa({},e),{},{playerMode:t.payload});case"[CORE] update video current fragment position":return fa(fa({},e),{},{currentVideoTimeFragment:t.payload});case"[CORE] update video current position":return fa(fa({},e),{},{currentVideoTime:t.payload});case"[CORE] update video current buffered time":return fa(fa({},e),{},{currentVideoBufferedTime:t.payload});case"[CORE] update video current duration":return fa(fa({},e),{},{currentVideoDuration:t.payload});case"[CORE] change video tag status":return fa(fa({},e),{},{videoTagStatus:t.payload});case"[CORE] update player visibility":return fa(fa({},e),{},{playerVisibility:t.payload});case"[CORE] update placeholder visibility":return fa(fa({},e),{},{playerPlaceholderVisibility:t.payload});case"[CORE] change loading player status":return fa(fa({},e),{},{loadingPlayer:t.payload});case"[COMMON] show black screen with loader":return fa(fa({},e),{},{loader:fa(fa({},e.loader),{},{showBlackScreen:t.payload})});case"[CORE] set player size":return fa(fa({},e),{},{playerSize:t.payload});case"[COMMON] set error message":return fa(fa({},e),{},{errorMessage:t.payload});default:return e}},brandingData:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:va,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return ga({},function(e,t){var n=t.powered_by_strip,r=t.brand_logo,i=t.brand_logo_click_url,o=t.brand_color;return ga(ga({},e),{},{showVoltaxLogo:Un(n)?e.showVoltaxLogo:n,brandingLogoSrc:Un(r)?e.brandingLogoSrc:r,brandingLogoUrl:Un(i)?e.brandingLogoUrl:i,brandingColor:Un(o)?e.brandingColor:o})}(e,t.payload.initiateParams));default:return e}},anchorOptions:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:Oa,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return ba({},function(e,t){var n=t.anchor_options;if(!Un(n)){var r=n.anchoring_appearance,i=n.can_close,o=n.closable_ad,a=n.close_after,s=n.continue_streaming,u=n.orientation,c=n.margins,l=n.sticky_below_class_name,d=n.width,p=Un(c)?e.margins:{top:Number.isInteger(c.top)?c.top:e.margins.top,bottom:Number.isInteger(c.bottom)?c.bottom:e.margins.bottom,left:Number.isInteger(c.left)?c.left:e.margins.left,right:Number.isInteger(c.right)?c.right:e.margins.right};return ba(ba({},e),{},{anchoringAppearance:r||e.anchoringAppearance,canClose:Un(i)?e.canClose:i,orientation:Un(u)?e.orientation:u,closableAd:Un(o)?e.closableAd:o,closeAfter:Un(a)?e.closeAfter:a,continueStreaming:Un(s)?e.continueStreaming:s,stickyBelowClassName:Un(l)?e.stickyBelowClassName:l,width:Un(d)?e.width:d,margins:p,anchorData:ba(ba({},e.anchorData),{},{anchorEnabled:!0})})}return e}(e,t.payload.initiateParams));case"[COMMON] set anchor enable":return ba(ba({},e),{},{anchorData:ba(ba({},e.anchorData),{},{anchorEnabled:t.payload})});case"[ANCHOR] update is anchor status":return ba(ba({},e),{},{anchorData:ba(ba({},e.anchorData),{},{anchorStatus:t.payload})});case"[COMMON] set anchor disabled by user":return ba(ba({},e),{},{anchorData:ba(ba({},e.anchorData),{},{anchorDisabledByUser:t.payload})});default:return e}},monetization:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:wa,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Sa({},function(e,t){var n=t.monetization;if(Un(n))return e;var r=n.ad_tag,i=n.ad_type,o=n.vpaid_mode,a=n.ad_request_timeout,s=n.continue_content_play_while_waiting_for_ad,u=n.midrolls,c=u&&u.on&&u.on.sort(Wn),l=Un(s)?e.continuePlayingWhileWaitingForAd:s,d=c?c.indexOf(0):-1,p=-1!==d&&!l;return p&&(c=c.splice(d,1)),Sa(Sa({},e),{},{midrolls:Sa(Sa({},e.midrolls),{},{every:u&&u.every,on:c}),prerollEnabled:p,adRequestTimeout:Un(a)?e.adRequestTimeout:parseInt(a,10),vpaidMode:Un(o)?e.vpaidMode:o,continuePlayingWhileWaitingForAd:l,adsData:Sa(Sa({},e.adsData),{},{adType:Un(i)?e.adsData.adType:i,adTagUrlTemplate:Un(r)?e.adsData.adTagUrlTemplate:r})})}(e,t.payload.initiateParams));case"[COMMON] set new ad tag url template":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adTagUrlTemplate:t.payload})});case"[MONETIZATION] change ad status":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adStatus:t.payload,adErrorMessage:null})});case"[MONETIZATION] change ad tag":var n=t.payload,r=n.adUnit,i=n.adTag;return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{currentAdTag:i,adUnit:r})});case"[MONETIZATION] change pending ad status":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{pendingAdStatus:t.payload})});case"[MONETIZATION] change ad error":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adStatus:"error",adErrorMessage:t.payload})});case"[MONETIZATION] increase ad impression counter":var o=e.adsData.adImpression;return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adImpression:o+1})});case"[MONETIZATION] increase ad Opportunity counter":var a=e.adsData.adOpportunity;return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adOpportunity:a+1})});case"[MONETIZATION] add played midroll number":var s=e.adsData.playedMidrolls,u=In()(s);return u.push(t.payload),Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adOrder:t.payload,playedMidrolls:u})});case"[MONETIZATION] clear played midrolls":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{playedMidrolls:[]})});case"[MONETIZATION] clear ad data":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adOrder:0,currentAdTag:null,adDuration:0,adUnit:""})});case"[MONETIZATION] change ad duration":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adDuration:t.payload})});case"[MONETIZATION] update is vast ad":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{isVastAd:t.payload})});case"[MONETIZATION] change ad current time":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adCurrentTime:t.payload})});case"[MONETIZATION] update ad muted":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adMuted:t.payload})});case"[MONETIZATION] change ad volume":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adVolume:t.payload})});case"[MONETIZATION] change pod info":var c=t.payload,l=c.podNumber,d=c.slotNumber;return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{podNumber:l,slotNumber:d})});case"[MONETIZATION] change loading ad status":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{loadingAd:t.payload})});default:return e}},mediaData:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:ja,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Va({},function(e,t){var n=t.content_type,r=t.media_id,i=t.display_title;return Va(Va({},e),{},{mediaType:Un(n)?e.mediaType:n,mediaId:Un(r)?e.mediaId:r,videoData:Va(Va({},e.videoData),{},{showTitle:!!Un(i)||i})})}(e,t.payload.initiateParams));case"[CORE] load video request":return Va(Va({},e),{},{loadingMedia:!0});case"[CORE] load video request success":return Va(Va({},e),{},{loadingMedia:!1,videoList:t.payload});case"[CORE] set current video":var n=t.payload,r=n.index,i=n.videoData;return Va(Va({},e),{},{activeVideoIndex:r,videoData:i});case"[CORE] load video request error":return Va(Va({},e),{},{loadingMedia:!1,mediaLoadingError:t.payload});case"[COMMON] media request":var o=t.payload.mediaRequestObject;return Va(Va({},e),{},{mediaRequest:Va({},o)});default:return e}},semanticOptions:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:Ba,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Fa({},function(e,t){var n=t.semantic_options;if(Un(n))return e;var r=n.minimum_date_factor,i=n.promoted_videos,o=n.scan_images_on_page,a=n.scanned_element,s=n.scanned_element_type,u=n.scoped_keywords,c=n.tags;return Fa(Fa({},e),{},{minimumDateFactor:Un(r)?e.minimumDateFactor:r,promotedVideos:Un(i)?e.promotedVideos:i,scanImagesOnPage:Un(o)?e.scanImagesOnPage:o,scannedElement:Un(a)?e.scannedElement:a,scannedElementType:Un(s)?e.scannedElementType:s,scopedKeywords:Un(u)?e.scopedKeywords:u,tags:Un(c)?e.tags:c})}(e,t.payload.initiateParams));default:return e}},userInteraction:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:Wa,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[USER INTERACTION] change user interaction":return qa(qa({},e),{},{userInteractionType:t.payload});default:return e}},splitView:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:$a,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Ga({},function(e,t){var n=t.anchor_options;if(!Un(n)){var r=n.split_view,i=n.split_view_ratio;return Ga(Ga({},e),{},{splitViewRatio:Un(r)||!r||Un(i)?e.splitViewRatio:i})}return e}(e,t.payload.initiateParams));default:return e}},discovery:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:Za,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Ya({},function(e,t){var n=t.next_video;return Un(n)?e:Ya(Ya({},e),{},{nextVideo:Xa(n)})}(e,t.payload.initiateParams));case"[DISCOVERY] show up next":return Ya(Ya({},e),{},{showUpNext:t.payload});case"[DISCOVERY] show skippable content":return Ya(Ya({},e),{},{showSkippableContent:t.payload});default:return e}}}),Qa=[],es=!1,ts=function e(){return function(t){return function(n){if(es)return Qa.push(n),null;es=!0;var r=t(n);return es=!1,Qa.length>0&&e()(t)(Qa.shift()),r}}},ns=function(e){var t=[];if(function(e){return!Un(e)&&!Un(e.enable_redux_debugging)&&e.enable_redux_debugging}(e)){var n=window&&window.__REDUX_DEVTOOLS_EXTENSION__&&window.__REDUX_DEVTOOLS_EXTENSION__();"function"===typeof n&&t.push(n)}var r=Et.apply(void 0,[wt(ua,ts)].concat(t));return vt(Ja,r)},rs=function(){function e(t){Ai()(this,e),f()(this,"playerVisibilitySubscriber",void 0),f()(this,"videoTagStatusSubscriber",void 0),f()(this,"shouldPlayIfLazyplay",!0),f()(this,"shouldPlayIfAutoplayWhenViewable",!0),f()(this,"videoPausedByObserver",!1),this.store=t,this.playerVisibilitySubscriber=null,this.videoTagStatusSubscriber=null,this.playAccordingToPlaybackMethod()}return Vi()(e,[{key:"lazyplayHandler",value:function(e){hn.playerVisibility(e)>=.5&&(this.playVideo(),this.shouldPlayIfLazyplay=!1)}},{key:"autoplayWhenViewableHandler",value:function(e){hn.playerVisibility(e)>=.5?this.playVideo():this.pauseVideo()}},{key:"onPlayerVisibilityChanged",value:function(e){var t=hn.playbackMethod(e);"lazyplay"===t&&this.shouldPlayIfLazyplay&&this.lazyplayHandler(e),"autoplay_when_viewable"===t&&this.shouldPlayIfAutoplayWhenViewable&&this.autoplayWhenViewableHandler(e)}},{key:"onVideoTagStatusChanged",value:function(e){var t=hn.videoTagStatus(e);"paused"!==t||this.videoPausedByObserver||(this.shouldPlayIfAutoplayWhenViewable=!1),"playing"===t&&(this.shouldPlayIfAutoplayWhenViewable=!0,this.videoPausedByObserver=!1)}},{key:"initiatePlayerVisibilitySubscriber",value:function(){this.playerVisibilitySubscriber=new ji(this.store,e.getPlayerVisibilityDependencies,this.onPlayerVisibilityChanged.bind(this))}},{key:"initiateVideoTagStatusSubscriber",value:function(){this.videoTagStatusSubscriber=new ji(this.store,e.getVideoTagStatusDependencies,this.onVideoTagStatusChanged.bind(this))}},{key:"playVideo",value:function(){var e=this.store,t=e.dispatch,n=e.getState;"idle"===hn.videoTagStatus(n())?on("play")(t):on("resume")(t)}},{key:"pauseVideo",value:function(){var e=this.store,t=e.dispatch,n=e.getState;"paused"!==hn.videoTagStatus(n())&&(this.videoPausedByObserver=!0,on("pause")(t))}},{key:"playAccordingToPlaybackMethod",value:function(){var e=this.store,t=e.dispatch,n=(0,e.getState)();switch(hn.playbackMethod(n)){case"autoplay":this.playVideo();break;case"lazyplay":this.initiatePlayerVisibilitySubscriber();break;case"autoplay_when_viewable":this.initiatePlayerVisibilitySubscriber(),this.initiateVideoTagStatusSubscriber();break;case"none":an(!1)(t)}}}],[{key:"getPlayerVisibilityDependencies",value:function(e){return[hn.playerVisibility(e)]}},{key:"getVideoTagStatusDependencies",value:function(e){return[hn.videoTagStatus(e)]}}]),e}(),is=function(){function e(t,n,r,i){var o=this;Ai()(this,e),f()(this,"videoStatusSubscriber",void 0),f()(this,"videoListSubscriber",void 0),f()(this,"mediaRequestSubscriber",void 0),f()(this,"playerVisibilitySubscriber",void 0),f()(this,"playbackMethodManager",void 0),f()(this,"store",void 0),f()(this,"loadContent",function(e,t,n,r){o.loadMedia(t,n,r).then(function(){o.playbackMethodManager=new rs(e)})}),f()(this,"loadMedia",function(e,t,n){var r=o.store,i=r.dispatch,a=r.getState,s=Dn.showTitle(a());if("semantic"===e){var u=pn.semanticOptions(a());return Na(u,s,n)(i)}return ka(t,s,n)(i)}),this.store=t,this.videoStatusSubscriber=new ji(t,e.getVideoStatusDependencies,this.onVideoStatusChanged.bind(this)),this.videoListSubscriber=new ji(t,e.getVideoListDependencies,this.onVideoListChanged.bind(this)),this.mediaRequestSubscriber=new ji(t,e.getMediaRequestDependencies,this.onMediaRequestChanged.bind(this)),this.playerVisibilitySubscriber=null,this.loadContent(t,r,n,i)}return Vi()(e,null,[{key:"createInstance",value:function(t,n,r,i){return new e(t,n,r,i)}}]),Vi()(e,[{key:"playNextVideo",value:function(e){var t=this.store.dispatch,n=Cn.videoList(e),r=Cn.activeVideoIndex(e)+1;n.length>1&&r>=n.length&&(r=0),r<n.length&&(!function(e){e({type:"[CORE] reset player data time params"})}(t),La(r,n[r])(t),on("play")(t))}},{key:"playPreviousVideo",value:function(e){var t=this.store.dispatch,n=Cn.videoList(e),r=Cn.activeVideoIndex(e);if(r>0){var i=r-1;La(i,n[i])(t),on("play")(t)}}},{key:"onVideoStatusChanged",value:function(e){"complete"===hn.videoTagStatus(e)&&this.playNextVideo(e)}},{key:"onVideoListChanged",value:function(e){var t=this.store.dispatch,n=Cn.videoList(e);!jn(n)&&n.length>0&&La(0,n[0])(t)}},{key:"onMediaRequestChanged",value:function(e){var t=Cn.mediaRequest(e);switch(t.type){case"playNewVideo":this.loadMedia("specific",t.value);break;case"playNextVideo":this.playNextVideo(e);break;case"playPreviousVideo":this.playPreviousVideo(e)}}}],[{key:"getVideoStatusDependencies",value:function(e){return[hn.videoTagStatus(e)]}},{key:"getVideoListDependencies",value:function(e){return[Cn.videoList(e)]}},{key:"getMediaRequestDependencies",value:function(e){return[Cn.mediaRequest(e)]}}]),e}(),os=function e(t){var n=this;Ai()(this,e),f()(this,"store",void 0),f()(this,"onDependencyFailure",function(e,t){console.log("onDependencyFailure",e,t);var r=n.store,i=r.dispatch,o=r.getState;switch(e){case"ima":"blocked"!==Fi.loadingImaStatus(o())&&Qn("error")(i);break;case"hls":er("error")(i)}}),f()(this,"onDependencyReady",function(e){var t=n.store.dispatch;switch(e){case"ima":Qn("success")(t);break;case"hls":er("success")(t)}}),this.store=t},as=function(e){return function(t){t({type:"[COMMON] set fullscreen",payload:e})}},ss=function(){function e(t,n){var r=this;Ai()(this,e),f()(this,"store",void 0),f()(this,"videoTag",void 0),f()(this,"pendingFullscreenSubscriber",void 0),f()(this,"adStatusSubscriber",void 0),f()(this,"playerUniqId",void 0),f()(this,"onAdStatusChanged",function(e){var t=_i.adStatus(e),n=r.videoTag.webkitDisplayingFullscreen;"playing"===t&&Bn()&&n&&r.exitFullscreen(r.videoTag)}),f()(this,"isPlayerInFullscreen",function(){var e=document,t=Bn()?En(r.playerUniqId):bn(r.playerUniqId);return Un(e.fullscreenElement)?!Un(e.webkitFullscreenElement)&&0===e.webkitFullscreenElement.id.localeCompare(t):0===e.fullscreenElement.id.localeCompare(t)}),f()(this,"changePlayerWidth",function(e){r.videoTag.style.width=e?"100%":"auto"}),f()(this,"onFullscreenChanged",function(){var e=r.store.dispatch,t=r.isPlayerInFullscreen();r.changePlayerWidth(t),as(t)(e)}),f()(this,"onFullscreenChangedIos",function(){var e=r.store.dispatch,t=r.videoTag.webkitDisplayingFullscreen;t||on("resume")(e),r.changePlayerWidth(t),as(t)(e)}),f()(this,"onPendingFullscreenRequestChanged",function(e){var t=gn.pendingFullscreenRequest(e);"enter"===t?r.enterFullscreen(r.videoTag):"exit"===t&&r.exitFullscreen(r.videoTag)}),f()(this,"getFullScreenElement",function(e,t){var n=document.getElementById(bn(r.playerUniqId));return Bn()?t:e?document:n}),f()(this,"enterFullscreen",function(e){var t=r.getFullScreenElement(!1,e);Bn()?t.webkitEnterFullscreen():document.webkitExitFullscreen?t.webkitRequestFullscreen():document.webkitCancelFullScreen?t.webkitRequestFullScreen():document.mozCancelFullScreen?t.mozRequestFullScreen():document.msExitFullscreen&&t.msRequestFullscreen()}),f()(this,"exitFullscreen",function(e){var t=r.getFullScreenElement(!0,e);document.webkitExitFullscreen||Bn()?t.webkitExitFullscreen():document.webkitCancelFullScreen?t.webkitCancelFullScreen():document.mozCancelFullScreen?t.mozCancelFullScreen():document.msExitFullscreen&&t.msExitFullscreen()}),this.store=t,this.videoTag=document.getElementById(En(n)),this.playerUniqId=n,document.addEventListener("fullscreenchange",this.onFullscreenChanged.bind(this)),document.addEventListener("webkitfullscreenchange",this.onFullscreenChanged.bind(this)),Bn()&&(this.videoTag.addEventListener("webkitendfullscreen",this.onFullscreenChangedIos.bind(this)),this.videoTag.addEventListener("webkitbeginfullscreen",this.onFullscreenChangedIos.bind(this))),this.pendingFullscreenSubscriber=new ji(t,e.getPendingFullscreenDependencies,this.onPendingFullscreenRequestChanged.bind(this)),this.adStatusSubscriber=new ji(t,e.getAdStatusDependencies,this.onAdStatusChanged.bind(this))}return Vi()(e,null,[{key:"createInstance",value:function(t,n){return new e(t,n)}}]),Vi()(e,null,[{key:"getPendingFullscreenDependencies",value:function(e){return[gn.pendingFullscreenRequest(e)]}},{key:"getAdStatusDependencies",value:function(e){return[_i.adStatus(e)]}}]),e}();function us(e,t){var n=Object.keys(e);if(Object.getOwnPropertySymbols){var r=Object.getOwnPropertySymbols(e);t&&(r=r.filter(function(t){return Object.getOwnPropertyDescriptor(e,t).enumerable})),n.push.apply(n,r)}return n}function cs(e){for(var t=1;t<arguments.length;t++){var n=null!=arguments[t]?arguments[t]:{};t%2?us(Object(n),!0).forEach(function(t){f()(e,t,n[t])}):Object.getOwnPropertyDescriptors?Object.defineProperties(e,Object.getOwnPropertyDescriptors(n)):us(Object(n)).forEach(function(t){Object.defineProperty(e,t,Object.getOwnPropertyDescriptor(n,t))})}return e}var ls,ds=function(e){return function(e){return e&&window.monti.playerConfigs&&window.monti.playerConfigs[e]}(e)?function(e){return 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t=hn.pendingVideoTagStatus(e),n=Dn.sources(e),i=Fi.loadingHLSStatus(e),o="blocked"===Fi.loadingImaStatus(e);r.handlePendingVideoStatus(t,n,i,o)}),f()(this,"onVideoDataChanged",function(){r.newVideoDataLoaded=!0}),f()(this,"sendPrerollPlayRequest",function(){var e=r.store.dispatch;hs("playPreroll")(e)}),f()(this,"handlePlayRequest",function(e,t,n){var i=r.store.dispatch;if(e&&e.length>0){if(r.newVideoDataLoaded&&(r.loadVideoSource(r.videoTag,e,t),r.newVideoDataLoaded=!1,r.prerollEnabled&&!n))return void r.sendPrerollPlayRequest();r.videoTag.play().catch(function(e){return console.error("Error playing the video: ",e)})}else dn(Xn.VIDEO_ERROR)(i)}),f()(this,"handlePendingVideoStatus",function(e,t,n,i){switch(e.type){case"play":r.handlePlayRequest(t,n,i);break;case"resume":r.videoTag.play().catch(function(e){return console.error("Error resuming the video: ",e)});break;case"pause":r.videoTag.pause();break;case"replay":r.videoTag.currentTime=0,r.videoTag.play().catch(function(e){return console.error("Error replaying the video: ",e)});break;case"seekTo":r.videoTag.pause(),r.videoTag.currentTime=e.value}}),f()(this,"loadMp4Source",function(e,t,n){var r=Ra(t,ys);n.setAttribute("src",r),n.load()}),f()(this,"loadVideoSource",function(e,t,n){var i=r.store.dispatch,o=Ra(t,gs);switch(fs.suitableVideoSource(e,o,n)){case"mp4":r.loadMp4Source(n,t,e);break;case"m3u8 with hls":r.videoStreamingManager.hlsLibrarySetup(e,o,function(e){return un(e)(i)},function(e){return dn(e)(i)});break;case"m3u8 directly":fs.loadHlsVideoDirectly(e,o)}}),this.store=t;var i=t.getState;this.videoStreamingManager=new fs,this.videoTag=document.getElementById(En(n)),this.prerollEnabled=bi.prerollEnabled(i()),this.pendingVideoStatusSubscriber=new ji(t,e.getPendingVideoStatusDependencies,this.onPendingVideoStatusChanged.bind(this)),this.videoDataSubscriber=new ji(t,e.getVideoDataDependencies,this.onVideoDataChanged.bind(this)),this.hlsLoadingStatusSubscriber=new ji(t,e.getHLSLoadingStatusDependencies,this.onHlsLoadingStatusChanged.bind(this))}return Vi()(e,null,[{key:"createInstance",value:function(t,n){return new e(t,n)}}]),Vi()(e,null,[{key:"getHLSLoadingStatusDependencies",value:function(e){return[Fi.loadingHLSStatus(e)]}},{key:"getPendingVideoStatusDependencies",value:function(e){return[hn.pendingVideoTagStatus(e)]}},{key:"getVideoDataDependencies",value:function(e){return[Cn.videoData(e)]}}]),e}();function ms(e,t){var n=Object.keys(e);if(Object.getOwnPropertySymbols){var r=Object.getOwnPropertySymbols(e);t&&(r=r.filter(function(t){return Object.getOwnPropertyDescriptor(e,t).enumerable})),n.push.apply(n,r)}return n}function bs(e){for(var t=1;t<arguments.length;t++){var n=null!=arguments[t]?arguments[t]:{};t%2?ms(Object(n),!0).forEach(function(t){f()(e,t,n[t])}):Object.getOwnPropertyDescriptors?Object.defineProperties(e,Object.getOwnPropertyDescriptors(n)):ms(Object(n)).forEach(function(t){Object.defineProperty(e,t,Object.getOwnPropertyDescriptor(n,t))})}return e}var Os={READY_EVENT:"ready",PLAY_EVENT:"play",PAUSE_EVENT:"pause",TIME_EVENT:"time",SEEK_EVENT:"seek",COMPLETE_EVENT:"complete",VOLUME_EVENT:"volume",MUTE_EVENT:"mute"},_s=Object.values(Os),Ss={FULLSCREEN_EVENT:"fullscreen",ANCHOR_STATUS_EVENT:"anchorStatusChanged",ANCHOR_CLOSED_EVENT:"anchorClosed"},Es={AD_PLAY_EVENT:"adPlay",AD_PAUSE_EVENT:"adPause",AD_RESUME_EVENT:"adResume",AD_COMPLETE_EVENT:"adComplete",AD_TIME_EVENT:"adTime",AD_MUTE_EVENT:"adMute",AD_SKIPPED_EVENT:"adSkipped",AD_ERROR_EVENT:"adError",AD_BLOCK_EVENT:"adBlock",AD_REQUEST_EVENT:"adRequest",AD_OPPORTUNITY_EVENT:"adOpportunity",AD_IMPRESSION_EVENT:"adImpression"},ws=Object.values(Es),Ps=Object.values(bs(bs(bs({},Os),Es),Ss)),Ts=function(){function e(t,n){var r=this;Ai()(this,e),f()(this,"eventsCallbacksHandler",void 0),f()(this,"store",void 0),f()(this,"videoStatusSubscriber",void 0),f()(this,"videoMuteSubscriber",void 0),f()(this,"videoVolumeSubscriber",void 0),f()(this,"videoTimeFragmentSubscriber",void 0),f()(this,"videoListStoreSubscriber",void 0),f()(this,"previousVideoTagStatus",void 0),f()(this,"startSeekTime",0),f()(this,"canHandleReady",function(e,t,n){if(t===Os.READY_EVENT){var r=Cn.videoList(e);if(Array.isArray(r)&&r.length>0)return n(),!0}return!1}),f()(this,"canBeHandled",function(e,t){var n=r.store.getState;return r.canHandleReady(n(),e,t)}),f()(this,"reportSeekEnd",function(e){var t={position:hn.currentVideoTimeFragment(e),offset:r.startSeekTime};r.eventsCallbacksHandler.onEvent(Os.SEEK_EVENT,t)}),f()(this,"onMuteStateChanged",function(e){var t=gn.muted(e);r.eventsCallbacksHandler.onEvent(Os.MUTE_EVENT,{state:t})}),f()(this,"onVolumeChanged",function(e){var t=gn.muted(e),n=gn.volume(e);r.eventsCallbacksHandler.onEvent(Os.VOLUME_EVENT,{level:t?0:n})}),f()(this,"onVideoTimeFragmentChanged",function(e){var t=hn.currentVideoTimeFragment(e),n=hn.currentVideoDuration(e);r.eventsCallbacksHandler.onEvent(Os.TIME_EVENT,{duration:n,position:t})}),f()(this,"onVideoListChanged",function(){r.eventsCallbacksHandler.onEvent(Os.READY_EVENT)}),this.store=t,this.eventsCallbacksHandler=n,this.videoStatusSubscriber=new ji(t,e.getVideoStatusDependencies,this.onVideoStatusChanged.bind(this)),this.videoMuteSubscriber=new ji(t,e.getVideoMuteDependencies,this.onMuteStateChanged.bind(this)),this.videoVolumeSubscriber=new ji(t,e.getVolumeDependencies,this.onVolumeChanged.bind(this)),this.videoTimeFragmentSubscriber=new ji(t,e.getVideoTimeDependencies,this.onVideoTimeFragmentChanged.bind(this)),this.videoListStoreSubscriber=new ji(t,e.getVideoListDependencies,this.onVideoListChanged.bind(this)),this.previousVideoTagStatus=hn.videoTagStatus(t.getState())}return Vi()(e,[{key:"onVideoStatusChanged",value:function(e){var t=hn.videoTagStatus(e);switch("seeking"===this.previousVideoTagStatus&&this.reportSeekEnd(e),t){case"paused":this.eventsCallbacksHandler.onEvent(Os.PAUSE_EVENT);break;case"seeking":this.startSeekTime=hn.currentVideoTimeFragment(e);break;case"complete":this.eventsCallbacksHandler.onEvent(Os.COMPLETE_EVENT);break;case"playing":this.eventsCallbacksHandler.onEvent(Os.PLAY_EVENT)}this.previousVideoTagStatus=t}}],[{key:"getVideoStatusDependencies",value:function(e){return[hn.videoTagStatus(e)]}}]),e}();f()(Ts,"getVideoMuteDependencies",function(e){return[gn.muted(e)]}),f()(Ts,"getVolumeDependencies",function(e){return[gn.volume(e)]}),f()(Ts,"getVideoTimeDependencies",function(e){return[hn.currentVideoTimeFragment(e)]}),f()(Ts,"getVideoListDependencies",function(e){return[Cn.videoList(e)]}),f()(Ts,"isContentEvent",function(e){return _s.some(function(t){return t===e})});var As=function e(t,n){var r=this;Ai()(this,e),f()(this,"eventsCallbacksHandler",void 0),f()(this,"store",void 0),f()(this,"fullscreenSubscriber",void 0),f()(this,"anchorStatusSubscriber",void 0),f()(this,"anchorDisabledByUserSubscriber",void 0),f()(this,"onFullscreenChanged",function(e){var t=gn.isFullscreenOn(e);r.eventsCallbacksHandler.onEvent(Ss.FULLSCREEN_EVENT,{state:t})}),f()(this,"onAnchorStatusChanged",function(e){var t="active"===Pr(e)?"activated":"deactivated";r.eventsCallbacksHandler.onEvent(Ss.ANCHOR_STATUS_EVENT,{state:t})}),f()(this,"onAnchorDisabledByUser",function(e){if(wr(e)){var t=hn.currentVideoTimeFragment(e);r.eventsCallbacksHandler.onEvent(Ss.ANCHOR_CLOSED_EVENT,{position:t})}}),this.store=t,this.eventsCallbacksHandler=n,this.fullscreenSubscriber=new ji(t,e.getFullscreenDependencies,this.onFullscreenChanged.bind(this)),this.anchorStatusSubscriber=new ji(t,e.getAnchorStatusDependencies,this.onAnchorStatusChanged.bind(this)),this.anchorDisabledByUserSubscriber=new 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t=_i.adStatus(e),n=_i.currentAdTag(e);switch(t){case"requested":r.eventsCallbacksHandler.onEvent(Es.AD_REQUEST_EVENT,{tag:n});break;case"paused":r.eventsCallbacksHandler.onEvent(Es.AD_PAUSE_EVENT,{tag:n});break;case"completed":r.eventsCallbacksHandler.onEvent(Es.AD_COMPLETE_EVENT,{tag:n});break;case"skipped":r.eventsCallbacksHandler.onEvent(Es.AD_SKIPPED_EVENT,{tag:n});break;case"playing":"paused"===r.previousAdStatus?r.eventsCallbacksHandler.onEvent(Es.AD_RESUME_EVENT,{tag:n}):r.eventsCallbacksHandler.onEvent(Es.AD_PLAY_EVENT,{tag:n});break;case"error":var i=_i.adErrorMessage(e);r.eventsCallbacksHandler.onEvent(Es.AD_ERROR_EVENT,{tag:n,message:i})}r.previousAdStatus=t}),f()(this,"onAtTimeChanged",function(e){var t=_i.adCurrentTime(e),n=_i.currentAdTag(e),i=_i.adDuration(e);r.eventsCallbacksHandler.onEvent(Es.AD_TIME_EVENT,{position:t,tag:n,duration:i})}),f()(this,"onAdMuteChanged",function(e){var t=_i.adMuted(e);r.eventsCallbacksHandler.onEvent(Es.AD_MUTE_EVENT,{state:t})}),f()(this,"onAdProviderLoadingChanged",function(e){"blocked"===Fi.loadingImaStatus(e)&&r.eventsCallbacksHandler.onEvent(Es.AD_BLOCK_EVENT)}),f()(this,"onAdImpressionChanged",function(e){var t=_i.currentAdTag(e);r.eventsCallbacksHandler.onEvent(Es.AD_IMPRESSION_EVENT,{tag:t})}),f()(this,"onAdOpportunityChanged",function(e){var t=_i.currentAdTag(e);r.eventsCallbacksHandler.onEvent(Es.AD_OPPORTUNITY_EVENT,{tag:t})}),this.store=t,this.eventsCallbacksHandler=n,this.previousAdStatus=_i.adStatus(t.getState()),this.adStatusSubscriber=new ji(t,e.getAdStatusDependencies,this.onAdStatusChanged.bind(this)),this.adTimeSubscriber=new ji(t,e.getAdTimeDependencies,this.onAtTimeChanged.bind(this)),this.adMuteSubscriber=new ji(t,e.getAdMuteDependencies,this.onAdMuteChanged.bind(this)),this.adImpressionSubscriber=new ji(t,e.getAdImpressionDependencies,this.onAdImpressionChanged.bind(this)),this.adOpportunitySubscriber=new 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{"is_conflicting_with_other_jw_players":false,"programmatic_play_with_sound_on_desktop":false,"referrer_id":"af93e181-b289-0560-a2bf-808e93bb05bc","width":"100","comscore_publisher_id":"18120612","monetization":{"ad_type":"static_tag","continue_content_play_while_waiting_for_ad":false,"strategy":"on_player_load","ad_request_timeout":"10000","midrolls":{"on":[0]},"vpaid_mode":"ENABLED","ad_tag":"https://pubads.g.doubleclick.net/gampad/ads?sz=400x300|640x480|480x270|640x360&iu=/175840252/MMPlus/smithsonianmag/Video&impl=s&gdfp_req=1&env=vp&output=vast&unviewed_position_start=1&url=##REFERRER_URL_UNESC##&description_url=##DESCRIPTION_URL_UNESC##&correlator=##CACHEBUSTER##&cust_params=mm_midroll%3D##MIDROLL_ORDER##%26video_ID%3D##VIDEO_ID##"},"sponsorship":false,"player_identifier":"mplayer","recommendation_id":null,"brand_color":"#FF9900","powered_by_strip":true,"platform":"buffy","type":"video","config_name":"MM+ | Smithsonianmag | Podding","player_id":"3v9g2u2f","playlist_id":"fSkmeWKF","playback_method":"autoplay","anchor_viewability_method":"none","player_version":"v4","playlist_type":"semantic","semantic_options":{"scan_images_on_page":true,"scanned_element":"","tags":"geogrophy,nature,animals,habitat,outdoors,science,history","minimum_date_factor":30,"scanned_element_type":"tag","scoped_keywords":"mentalfloss","promoted_videos":[]},"script_destination":"mm","publisher_contribution":"floor8","general_script_description":"","brand_logo":"","brand_logo_click_url":"","next_video":"none","uniq_key":"af93e181-b289-0560-a2bf-808e93bb05bc","content_id":"fSkmeWKF","content_type":"semantic"})); Finland has vastly improved in reading, math and science literacy over the past decade in large part because its teachers are trusted to do whatever it takes to turn young lives around. This 13-year-old, Besart Kabashi, received something akin to royal tutoring. “I took Besart on that year as my private student,” Louhivuori told me in his office, which boasted a Beatles “Yellow Submarine” poster on the wall and an electric guitar in the closet. When Besart was not studying science, geography and math, he was parked next to Louhivuori’s desk at the front of his class of 9- and 10-year- olds, cracking open books from a tall stack, slowly reading one, then another, then devouring them by the dozens. By the end of the year, the son of Kosovo war refugees had conquered his adopted country’s vowel-rich language and arrived at the realization that he could, in fact, learn. Years later, a 20-year-old Besart showed up at Kirkkojarvi’s Christmas party with a bottle of Cognac and a big grin. “You helped me,” he told his former teacher. Besart had opened his own car repair firm and a cleaning company. “No big fuss,” Louhivuori told me. “This is what we do every day, prepare kids for life.” This tale of a single rescued child hints at some of the reasons for the tiny Nordic nation’s staggering record of education success, a phenomenon that has inspired, baffled and even irked many of America’s parents and educators. Finnish schooling became an unlikely hot topic after the 2010 documentary film Waiting for “Superman” contrasted it with America’s troubled public schools. “Whatever it takes” is an attitude that drives not just Kirkkojarvi’s 30 teachers, but most of Finland’s 62,000 educators in 3,500 schools from Lapland to Turku—professionals selected from the top 10 percent of the nation’s graduates to earn a required master’s degree in education. Many schools are small enough so that teachers know every student. If one method fails, teachers consult with colleagues to try something else. They seem to relish the challenges. Nearly 30 percent of Finland’s children receive some kind of special help during their first nine years of school. The school where Louhivuori teaches served 240 first through ninth graders last year; and in contrast with Finland’s reputation for ethnic homogeneity, more than half of its 150 elementary-level students are immigrants—from Somalia, Iraq, Russia, Bangladesh, Estonia and Ethiopia, among other nations. “Children from wealthy families with lots of education can be taught by stupid teachers,” Louhivuori said, smiling. “We try to catch the weak students. It’s deep in our thinking.” Advertisement scroll for more The transformation of the Finns’ education system began some 40 years ago as the key propellent of the country’s economic recovery plan. Educators had little idea it was so successful until 2000, when the first results from the Programme for International Student Assessment (PISA), a standardized test given to 15-year-olds in more than 40 global venues, revealed Finnish youth to be the best young readers in the world. Three years later, they led in math. By 2006, Finland was first out of 57 countries (and a few cities) in science. In the 2009 PISA scores released last year, the nation came in second in science, third in reading and sixth in math among nearly half a million students worldwide. “I’m still surprised,” said Arjariita Heikkinen, principal of a Helsinki comprehensive school. “I didn’t realize we were that good.” In the United States, which has muddled along in the middle for the past decade, government officials have attempted to introduce marketplace competition into public schools. In recent years, a group of Wall Street financiers and philanthropists such as Bill Gates have put money behind private-sector ideas, such as vouchers, data-driven curriculum and charter schools, which have doubled in number in the past decade. President Obama, too, has apparently bet on competition. His Race to the Top initiative invites states to compete for federal dollars using tests and other methods to measure teachers, a philosophy that would not fly in Finland. “I think, in fact, teachers would tear off their shirts,” said Timo Heikkinen, a Helsinki principal with 24 years of teaching experience. “If you only measure the statistics, you miss the human aspect.”
The facts show that America has it all wrong in putting to much emphasis on national "data-driven" competition. These approaches take away from the unique aspects of each child.
t was the end of term at Kirkkojarvi Comprehensive School in Espoo, a sprawling suburb west of Helsinki, when Kari Louhivuori, a veteran teacher and the school’s principal, decided to try something extreme—by Finnish standards. One of his sixth-grade students, a Kosovo-Albanian boy, had drifted far off the learning grid, resisting his teacher’s best efforts. The school’s team of special educators—including a social worker, a nurse and a psychologist—convinced Louhivuori that laziness was not to blame. 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n=r.generatePrerollTag(e,t);r.monetization.onPrerollAdOpportunity(n)}),f()(this,"onSeekedWhileAdInProgress",function(){r.monetization.onMidrollAdOpportunity()});var i=t.getState;this.monetization=n,this.videoTimeSubscriber=new qi(t,this),this.videoSeekSubscriber=new zi(t,this),this.prerollScheduler=new Gi(t,this);var o=_i.adTagUrlTemplate(i());this.adTagGenerator=new Wi(o)},Yi=function(){function e(){Ai()(this,e)}return Vi()(e,null,[{key:"generateAdRequest",value:function(e,t,n){var r=new google.ima.AdsRequest;return r.adTagUrl=e,Fn()||r.setAdWillPlayMuted(t),r.vastLoadTimeout=n,r}}]),e}(),Zi=function(e){return function(t){t({type:"[MONETIZATION] change ad status",payload:e})}},Xi=function(e){return function(t){t({type:"[COMMON] set pending video status",payload:{pendingStatusObject:{type:e,value:""}}})}},Ji=function(e){return function(t){t({type:"[MONETIZATION] change loading ad status",payload:e})}},Qi=function(e){return function(t){t({type:"[MONETIZATION] update ad 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t=a.store,n=t.getState,r=t.dispatch,i=gn.volume(n());Bn()||gn.muted(n())?(e.setVolume(0),Qi(!0)(r)):(e.setVolume(gn.volume(n())),eo(i)(r),Qi(!1)(r))}),f()(this,"createIMAAdManager",function(t){a.IMAAdManager=t.getAdsManager(a.adVideoElement,e.getAdsRenderingSettings()),a.setAdVolume(a.IMAAdManager)}),f()(this,"registerToAdManagerEvents",function(){a.IMAAdManager.addEventListener(google.ima.AdErrorEvent.Type.AD_ERROR,a.onAdError),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.CONTENT_PAUSE_REQUESTED,a.onContentPauseRequested),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.CONTENT_RESUME_REQUESTED,a.onContentResumeRequested),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.STARTED,a.onAdStarted),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.IMPRESSION,a.onAdImpression),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.SKIPPED,a.onAdSkipped),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.COMPLETE,a.onAdCompleted),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.PAUSED,a.onAdPaused),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.RESUMED,a.onAdStarted),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.AD_PROGRESS,a.onAdProgressChanged),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.VOLUME_CHANGED,a.onVolumeChanged),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.VOLUME_MUTED,a.onAdVolumeMutedChanged),a.IMAAdManager.addEventListener(google.ima.AdEvent.Type.ALL_ADS_COMPLETED,a.onAdCompleted)}),f()(this,"onIMAAdsManagerLoaded",function(e){var t=a.store.dispatch;a.createIMAAdManager(e),a.registerToAdManagerEvents(),Zi("loaded")(t)}),f()(this,"onAdError",function(e){var t=a.store.dispatch;!function(e){return function(t){t({type:"[MONETIZATION] change ad error",payload:e})}}(e.getError().getMessage())(t),Ji(!1),a.continuePlayingContent()}),f()(this,"onAdImpression",function(e){var t=a.store.dispatch,n=!e.getAd().g.vpaid;a.setPodInfo(e),function(e){e({type:"[MONETIZATION] increase ad impression counter"})}(t),function(e){return function(t){t({type:"[MONETIZATION] update is vast ad",payload:e})}}(n)(t)}),f()(this,"onVolumeChanged",function(e){var t=a.store.dispatch;eo(e.target.getVolume())(t)}),f()(this,"onAdVolumeMutedChanged",function(e){var t=a.store.dispatch;0===e.target.getVolume()?Qi(!0)(t):Qi(!1)(t)}),f()(this,"continuePlayingContent",function(){var e=a.store,t=e.getState,n=e.dispatch,r=hn.videoTagStatus(t());Xi("idle"===r?"play":"resume")(n)}),f()(this,"stopPlayingContent",function(){var 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e=a.store.dispatch;Zi("skipped")(e)}),f()(this,"onResize",function(){Un(a.IMAAdManager)||(a.IMAAdManager.resize(a.videoPlayerElement.clientWidth,a.videoPlayerElement.clientHeight,google.ima.ViewMode.NORMAL),a.adContainerElement.style.height="".concat(a.videoPlayerElement.clientHeight,"px"))}),f()(this,"onAdProgressChanged",function(e){var t,n,r=a.store,i=r.dispatch,o=r.getState,s=e.getAdData().currentTime,u=e.getAdData().duration,c=_i.adDuration(o());(t=s,function(e){e({type:"[MONETIZATION] change ad current time",payload:t})})(i),c!==u&&(n=u,function(e){e({type:"[MONETIZATION] change ad duration",payload:n})})(i)}),f()(this,"onAnchorStatusChanged",function(){var e=a.store.getState;"processing"!==Pr(e())&&a.onResize()}),f()(this,"changeAdVolume",function(e){Un(a.IMAAdManager)||a.IMAAdManager.setVolume(e)}),f()(this,"changeAdMuted",function(e,t){Un(a.IMAAdManager)||(t?a.IMAAdManager.setVolume(0):a.IMAAdManager.setVolume(e))}),f()(this,"changeAdStatus",function(e){Un(a.IMAAdManager)||("playing"===e&&a.IMAAdManager.resume(),"paused"===e&&a.IMAAdManager.pause())});var s=t.getState;this.store=t,this.adVideoElement=r,this.videoPlayerElement=i,this.adContainerElement=n,this.adDisplayContainer=new google.ima.AdDisplayContainer(n,r),this.createAdLoader(s(),this.adDisplayContainer),this.adDisplayContainer.initialize(),this.anchorStatusStoreSubscriber=new ji(t,e.getAnchorDependencies,this.onAnchorStatusChanged.bind(this)),this.registerForWindowResize(),this.initMutationObserver(o)};f()(to,"getAdsRenderingSettings",function(){var e=new google.ima.AdsRenderingSettings;return 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e=s.store,t=e.dispatch,n=e.getState,r=_i.adStatus(n()),i=bi.continuePlayingWhileWaitingForAd(n());"loaded"===r?s.playAd(!0):"requested"===r&&(s.pendingMidrollAdPlay=!0,i||(Xi("pause")(t),Ji(!0)(t))),function(e){e({type:"[MONETIZATION] increase ad Opportunity counter"})}(t)}),f()(this,"onPrerollAdOpportunity",function(e){var t=s.store,n=t.getState,r=t.dispatch,i=Fi.loadingImaStatus(n());Un(s.adHandler)?"loading"!==i&&""!==i||(Ji(!0)(r),s.pendingPrerollAdPlay=!0,s.pendingPrerollAdTag=e):(s.pendingPrerollAdPlay=!0,Ji(!0)(r),s.adHandler.loadNewAd(e,"preroll"))}),f()(this,"onPreMidrollAdOpportunity",function(e,t){Un(s.adHandler)||(e.currentTime>=e.midrollTime&&(s.pendingMidrollAdPlay=!0),s.pendingMidrollNumber=e.midrollNumber,s.adHandler.loadNewAd(t,"midroll"))}),f()(this,"hasPendingAd",function(){return s.hasPendingMidrollAdPlay()||s.hasPendingPrerollAdPlay()}),f()(this,"onAdStatusChanged",function(e){var t=s.store.dispatch,n=_i.adStatus(e);"completed"===n&&Ji(!1)(t);var r=bi.continuePlayingWhileWaitingForAd(e),i=_i.loadingAd(e);"playing"!==n&&"error"!==n||r||!i||Ji(!1)(t),s.hasPendingAd()&&"loaded"===n?s.playAd(s.hasPendingMidrollAdPlay()):s.hasPendingAd()&&"error"===n?(Ji(!1),s.clearPendingMidroll(),s.clearPendingPreroll()):Hi(n)||(Ji(!1),function(e){e({type:"[MONETIZATION] clear ad data"})}(t))}),f()(this,"clearPendingMidroll",function(){s.pendingMidrollNumber=null,s.pendingMidrollAdPlay=!1}),f()(this,"clearPendingPreroll",function(){s.pendingPrerollAdPlay=!1,s.pendingPrerollAdTag=null}),f()(this,"onVideoTagStatusChanged",function(e){"complete"===hn.videoTagStatus(e)&&function(e){e({type:"[MONETIZATION] clear played midrolls"})}(s.store.dispatch)}),f()(this,"hasPendingMidrollAdPlay",function(){return s.pendingMidrollAdPlay}),f()(this,"hasPendingPrerollAdPlay",function(){return s.pendingPrerollAdPlay}),f()(this,"playAd",function(e){var t,n=s.store.dispatch,r=s.adHandler.playAd();e?((t=s.pendingMidrollNumber,function(e){e({type:"[MONETIZATION] add 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Ki(t,this),this.adStatusSubscriber=new ji(t,e.getAdStatusDependencies,this.onAdStatusChanged.bind(this)),this.videoTagStatusSubscriber=new ji(t,e.getVideoTagStatusDependencies,this.onVideoTagStatusChanged.bind(this)),e.canUseIMA(u())?this.adHandler=new to(t,r,i,o,a):this.imaLoadingStatusSubscriber=new ji(t,e.getIMALoadingStatusDependencies,this.onIMALoadingStatusChanged.bind(this)),this.pendingAdStatusStoreSubscriber=new ji(t,e.getPendingAdStatusDependencies,this.onPendingAdStatusChanged.bind(this)),this.adMutedStoreSubscriber=new ji(t,e.getAdMutedDependencies,this.onAdMutedChanged.bind(this)),this.adVolumeStoreSubscriber=new ji(t,e.getAdVolumeDependencies,this.onAdVolumeChanged.bind(this))};f()(no,"getAdStatusDependencies",function(e){return[_i.adStatus(e)]}),f()(no,"getVideoTagStatusDependencies",function(e){return[hn.videoTagStatus(e)]}),f()(no,"getIMALoadingStatusDependencies",function(e){return[Fi.loadingImaStatus(e)]}),f()(no,"canUseIMA",function(e){return"success"===Fi.loadingImaStatus(e)}),f()(no,"getPendingAdStatusDependencies",function(e){return[_i.pendingAdStatus(e)]}),f()(no,"getAdMutedDependencies",function(e){return[_i.adMuted(e)]}),f()(no,"getAdVolumeDependencies",function(e){return[_i.adVolume(e)]});var ro=function(e,t){!function(e,t){var n=document.getElementById(vn(t));B(b(Li,{store:e,playerId:t}),n)}(e,t);var n=function(e){var t=Ri(e);return document.getElementById(t)}(t),r=function(e){var t=Bn()?Di(e):En(e);return document.getElementById(t)}(t),i=function(e){var t=En(e);return document.getElementById(t)}(t),o=function(e){var t=bn(e);return document.getElementById(t)}(t);return new 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this.errorMessage=e,this}},{key:"setAdPodNumber",value:function(e){return this.adPodNumber=e,this}},{key:"setAdSlotNumber",value:function(e){return this.adSlotNumber=e,this}},{key:"build",value:function(){var e=[];return jn(this.position)||e.push("video current position=".concat(Hn(this.position),"sec")),jn(this.duration)||e.push("video duration time=".concat(Hn(this.duration),"sec")),jn(this.loadTime)||e.push("video load time=".concat(this.loadTime,"milliseconds")),jn(this.previousPosition)||e.push("previous position=".concat(Hn(this.previousPosition),"sec")),jn(this.adOrder)||e.push("ad order=".concat(this.adOrder)),jn(this.adType)||e.push("ad type=".concat(this.adType)),jn(this.adDuration)||e.push("ad duration=".concat(Hn(Number(this.adDuration)),"sec")),jn(this.adPodNumber)||e.push("pod number=".concat(this.adPodNumber)),jn(this.adSlotNumber)||e.push("slot number=".concat(this.adSlotNumber)),jn(this.errorMessage)||e.push("error 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The initial state may not be undefined, but can be null.')})}(n)}catch(s){o=s}return function(e,t){if(void 0===e&&(e={}),o)throw o;for(var r=!1,i={},s=0;s<a.length;s++){var u=a[s],c=n[u],l=e[u],d=c(l,t);if("undefined"===typeof d){var p=mt(u,t);throw new Error(p)}i[u]=d,r=r||d!==l}return(r=r||a.length!==Object.keys(e).length)?i:e}}({dependenciesLoadingStatus:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:da,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] update hls status":return la(la({},e),{},{loadingHLSStatus:t.payload});case"[CORE] update ima status":return la(la({},e),{},{loadingImaStatus:t.payload});default:return e}},playerData:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:ha,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":var n=t.payload;return fa({},function(e,t,n){var r=t.playback_method,i=t.player_id;return fa(fa({},e),{},{playbackMethod:Un(r)?e.playbackMethod:r,playerId:Un(i)?e.playerId:i,playerInstanceUniqId:n,playerMode:Fn()?"mobile":"desktop"})}(e,n.initiateParams,n.playerInstanceUniqId));case"[CORE] reset player data time params":return fa(fa({},e),{},{currentVideoTimeFragment:0,currentVideoBufferedTime:0,currentVideoDuration:0,currentVideoTime:0});case"[COMMON] set mute video":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{muted:t.payload})});case"[COMMON] set volume":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{volume:t.payload})});case"[COMMON] change selected settings category":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{selectedSettingsCategory:t.payload})});case"[COMMON] change settings speed":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{speed:t.payload})});case"[COMMON] change settings quality":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{quality:t.payload})});case"[COMMON] set fullscreen":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{fullscreen:fa(fa({},e.playerSettings.fullscreen),{},{isFullscreenOn:t.payload,pendingFullscreenRequest:""})})});case"[COMMON] set fullscreen request":return fa(fa({},e),{},{playerSettings:fa(fa({},e.playerSettings),{},{fullscreen:fa(fa({},e.playerSettings.fullscreen),{},{pendingFullscreenRequest:t.payload})})});case"[COMMON] set pending video status":var r=t.payload.pendingStatusObject;return fa(fa({},e),{},{pendingVideoTagStatus:fa({},r)});case"[COMMON] set player mode":return fa(fa({},e),{},{playerMode:t.payload});case"[CORE] update video current fragment position":return fa(fa({},e),{},{currentVideoTimeFragment:t.payload});case"[CORE] update video current position":return fa(fa({},e),{},{currentVideoTime:t.payload});case"[CORE] update video current buffered time":return fa(fa({},e),{},{currentVideoBufferedTime:t.payload});case"[CORE] update video current duration":return fa(fa({},e),{},{currentVideoDuration:t.payload});case"[CORE] change video tag status":return fa(fa({},e),{},{videoTagStatus:t.payload});case"[CORE] update player visibility":return fa(fa({},e),{},{playerVisibility:t.payload});case"[CORE] update placeholder visibility":return fa(fa({},e),{},{playerPlaceholderVisibility:t.payload});case"[CORE] change loading player status":return fa(fa({},e),{},{loadingPlayer:t.payload});case"[COMMON] show black screen with loader":return fa(fa({},e),{},{loader:fa(fa({},e.loader),{},{showBlackScreen:t.payload})});case"[CORE] set player size":return fa(fa({},e),{},{playerSize:t.payload});case"[COMMON] set error message":return fa(fa({},e),{},{errorMessage:t.payload});default:return e}},brandingData:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:va,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return ga({},function(e,t){var n=t.powered_by_strip,r=t.brand_logo,i=t.brand_logo_click_url,o=t.brand_color;return ga(ga({},e),{},{showVoltaxLogo:Un(n)?e.showVoltaxLogo:n,brandingLogoSrc:Un(r)?e.brandingLogoSrc:r,brandingLogoUrl:Un(i)?e.brandingLogoUrl:i,brandingColor:Un(o)?e.brandingColor:o})}(e,t.payload.initiateParams));default:return e}},anchorOptions:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:Oa,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return ba({},function(e,t){var n=t.anchor_options;if(!Un(n)){var r=n.anchoring_appearance,i=n.can_close,o=n.closable_ad,a=n.close_after,s=n.continue_streaming,u=n.orientation,c=n.margins,l=n.sticky_below_class_name,d=n.width,p=Un(c)?e.margins:{top:Number.isInteger(c.top)?c.top:e.margins.top,bottom:Number.isInteger(c.bottom)?c.bottom:e.margins.bottom,left:Number.isInteger(c.left)?c.left:e.margins.left,right:Number.isInteger(c.right)?c.right:e.margins.right};return ba(ba({},e),{},{anchoringAppearance:r||e.anchoringAppearance,canClose:Un(i)?e.canClose:i,orientation:Un(u)?e.orientation:u,closableAd:Un(o)?e.closableAd:o,closeAfter:Un(a)?e.closeAfter:a,continueStreaming:Un(s)?e.continueStreaming:s,stickyBelowClassName:Un(l)?e.stickyBelowClassName:l,width:Un(d)?e.width:d,margins:p,anchorData:ba(ba({},e.anchorData),{},{anchorEnabled:!0})})}return e}(e,t.payload.initiateParams));case"[COMMON] set anchor enable":return ba(ba({},e),{},{anchorData:ba(ba({},e.anchorData),{},{anchorEnabled:t.payload})});case"[ANCHOR] update is anchor status":return ba(ba({},e),{},{anchorData:ba(ba({},e.anchorData),{},{anchorStatus:t.payload})});case"[COMMON] set anchor disabled by user":return ba(ba({},e),{},{anchorData:ba(ba({},e.anchorData),{},{anchorDisabledByUser:t.payload})});default:return e}},monetization:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:wa,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Sa({},function(e,t){var n=t.monetization;if(Un(n))return e;var r=n.ad_tag,i=n.ad_type,o=n.vpaid_mode,a=n.ad_request_timeout,s=n.continue_content_play_while_waiting_for_ad,u=n.midrolls,c=u&&u.on&&u.on.sort(Wn),l=Un(s)?e.continuePlayingWhileWaitingForAd:s,d=c?c.indexOf(0):-1,p=-1!==d&&!l;return p&&(c=c.splice(d,1)),Sa(Sa({},e),{},{midrolls:Sa(Sa({},e.midrolls),{},{every:u&&u.every,on:c}),prerollEnabled:p,adRequestTimeout:Un(a)?e.adRequestTimeout:parseInt(a,10),vpaidMode:Un(o)?e.vpaidMode:o,continuePlayingWhileWaitingForAd:l,adsData:Sa(Sa({},e.adsData),{},{adType:Un(i)?e.adsData.adType:i,adTagUrlTemplate:Un(r)?e.adsData.adTagUrlTemplate:r})})}(e,t.payload.initiateParams));case"[COMMON] set new ad tag url template":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adTagUrlTemplate:t.payload})});case"[MONETIZATION] change ad status":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adStatus:t.payload,adErrorMessage:null})});case"[MONETIZATION] change ad tag":var n=t.payload,r=n.adUnit,i=n.adTag;return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{currentAdTag:i,adUnit:r})});case"[MONETIZATION] change pending ad status":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{pendingAdStatus:t.payload})});case"[MONETIZATION] change ad error":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adStatus:"error",adErrorMessage:t.payload})});case"[MONETIZATION] increase ad impression counter":var o=e.adsData.adImpression;return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adImpression:o+1})});case"[MONETIZATION] increase ad Opportunity counter":var a=e.adsData.adOpportunity;return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adOpportunity:a+1})});case"[MONETIZATION] add played midroll number":var s=e.adsData.playedMidrolls,u=In()(s);return u.push(t.payload),Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adOrder:t.payload,playedMidrolls:u})});case"[MONETIZATION] clear played midrolls":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{playedMidrolls:[]})});case"[MONETIZATION] clear ad data":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adOrder:0,currentAdTag:null,adDuration:0,adUnit:""})});case"[MONETIZATION] change ad duration":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adDuration:t.payload})});case"[MONETIZATION] update is vast ad":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{isVastAd:t.payload})});case"[MONETIZATION] change ad current time":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adCurrentTime:t.payload})});case"[MONETIZATION] update ad muted":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adMuted:t.payload})});case"[MONETIZATION] change ad volume":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{adVolume:t.payload})});case"[MONETIZATION] change pod info":var c=t.payload,l=c.podNumber,d=c.slotNumber;return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{podNumber:l,slotNumber:d})});case"[MONETIZATION] change loading ad status":return Sa(Sa({},e),{},{adsData:Sa(Sa({},e.adsData),{},{loadingAd:t.payload})});default:return e}},mediaData:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:ja,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Va({},function(e,t){var n=t.content_type,r=t.media_id,i=t.display_title;return Va(Va({},e),{},{mediaType:Un(n)?e.mediaType:n,mediaId:Un(r)?e.mediaId:r,videoData:Va(Va({},e.videoData),{},{showTitle:!!Un(i)||i})})}(e,t.payload.initiateParams));case"[CORE] load video request":return Va(Va({},e),{},{loadingMedia:!0});case"[CORE] load video request success":return Va(Va({},e),{},{loadingMedia:!1,videoList:t.payload});case"[CORE] set current video":var n=t.payload,r=n.index,i=n.videoData;return Va(Va({},e),{},{activeVideoIndex:r,videoData:i});case"[CORE] load video request error":return Va(Va({},e),{},{loadingMedia:!1,mediaLoadingError:t.payload});case"[COMMON] media request":var o=t.payload.mediaRequestObject;return Va(Va({},e),{},{mediaRequest:Va({},o)});default:return e}},semanticOptions:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:Ba,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Fa({},function(e,t){var n=t.semantic_options;if(Un(n))return e;var r=n.minimum_date_factor,i=n.promoted_videos,o=n.scan_images_on_page,a=n.scanned_element,s=n.scanned_element_type,u=n.scoped_keywords,c=n.tags;return Fa(Fa({},e),{},{minimumDateFactor:Un(r)?e.minimumDateFactor:r,promotedVideos:Un(i)?e.promotedVideos:i,scanImagesOnPage:Un(o)?e.scanImagesOnPage:o,scannedElement:Un(a)?e.scannedElement:a,scannedElementType:Un(s)?e.scannedElementType:s,scopedKeywords:Un(u)?e.scopedKeywords:u,tags:Un(c)?e.tags:c})}(e,t.payload.initiateParams));default:return e}},userInteraction:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:Wa,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[USER INTERACTION] change user interaction":return qa(qa({},e),{},{userInteractionType:t.payload});default:return e}},splitView:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:$a,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Ga({},function(e,t){var n=t.anchor_options;if(!Un(n)){var r=n.split_view,i=n.split_view_ratio;return Ga(Ga({},e),{},{splitViewRatio:Un(r)||!r||Un(i)?e.splitViewRatio:i})}return e}(e,t.payload.initiateParams));default:return e}},discovery:function(){var e=arguments.length>0&&void 0!==arguments[0]?arguments[0]:Za,t=arguments.length>1?arguments[1]:void 0;switch(t.type){case"[CORE] initiate store":return Ya({},function(e,t){var n=t.next_video;return Un(n)?e:Ya(Ya({},e),{},{nextVideo:Xa(n)})}(e,t.payload.initiateParams));case"[DISCOVERY] show up next":return Ya(Ya({},e),{},{showUpNext:t.payload});case"[DISCOVERY] show skippable content":return Ya(Ya({},e),{},{showSkippableContent:t.payload});default:return e}}}),Qa=[],es=!1,ts=function e(){return function(t){return function(n){if(es)return Qa.push(n),null;es=!0;var r=t(n);return es=!1,Qa.length>0&&e()(t)(Qa.shift()),r}}},ns=function(e){var t=[];if(function(e){return!Un(e)&&!Un(e.enable_redux_debugging)&&e.enable_redux_debugging}(e)){var n=window&&window.__REDUX_DEVTOOLS_EXTENSION__&&window.__REDUX_DEVTOOLS_EXTENSION__();"function"===typeof n&&t.push(n)}var r=Et.apply(void 0,[wt(ua,ts)].concat(t));return vt(Ja,r)},rs=function(){function e(t){Ai()(this,e),f()(this,"playerVisibilitySubscriber",void 0),f()(this,"videoTagStatusSubscriber",void 0),f()(this,"shouldPlayIfLazyplay",!0),f()(this,"shouldPlayIfAutoplayWhenViewable",!0),f()(this,"videoPausedByObserver",!1),this.store=t,this.playerVisibilitySubscriber=null,this.videoTagStatusSubscriber=null,this.playAccordingToPlaybackMethod()}return Vi()(e,[{key:"lazyplayHandler",value:function(e){hn.playerVisibility(e)>=.5&&(this.playVideo(),this.shouldPlayIfLazyplay=!1)}},{key:"autoplayWhenViewableHandler",value:function(e){hn.playerVisibility(e)>=.5?this.playVideo():this.pauseVideo()}},{key:"onPlayerVisibilityChanged",value:function(e){var t=hn.playbackMethod(e);"lazyplay"===t&&this.shouldPlayIfLazyplay&&this.lazyplayHandler(e),"autoplay_when_viewable"===t&&this.shouldPlayIfAutoplayWhenViewable&&this.autoplayWhenViewableHandler(e)}},{key:"onVideoTagStatusChanged",value:function(e){var t=hn.videoTagStatus(e);"paused"!==t||this.videoPausedByObserver||(this.shouldPlayIfAutoplayWhenViewable=!1),"playing"===t&&(this.shouldPlayIfAutoplayWhenViewable=!0,this.videoPausedByObserver=!1)}},{key:"initiatePlayerVisibilitySubscriber",value:function(){this.playerVisibilitySubscriber=new ji(this.store,e.getPlayerVisibilityDependencies,this.onPlayerVisibilityChanged.bind(this))}},{key:"initiateVideoTagStatusSubscriber",value:function(){this.videoTagStatusSubscriber=new ji(this.store,e.getVideoTagStatusDependencies,this.onVideoTagStatusChanged.bind(this))}},{key:"playVideo",value:function(){var e=this.store,t=e.dispatch,n=e.getState;"idle"===hn.videoTagStatus(n())?on("play")(t):on("resume")(t)}},{key:"pauseVideo",value:function(){var e=this.store,t=e.dispatch,n=e.getState;"paused"!==hn.videoTagStatus(n())&&(this.videoPausedByObserver=!0,on("pause")(t))}},{key:"playAccordingToPlaybackMethod",value:function(){var e=this.store,t=e.dispatch,n=(0,e.getState)();switch(hn.playbackMethod(n)){case"autoplay":this.playVideo();break;case"lazyplay":this.initiatePlayerVisibilitySubscriber();break;case"autoplay_when_viewable":this.initiatePlayerVisibilitySubscriber(),this.initiateVideoTagStatusSubscriber();break;case"none":an(!1)(t)}}}],[{key:"getPlayerVisibilityDependencies",value:function(e){return[hn.playerVisibility(e)]}},{key:"getVideoTagStatusDependencies",value:function(e){return[hn.videoTagStatus(e)]}}]),e}(),is=function(){function e(t,n,r,i){var o=this;Ai()(this,e),f()(this,"videoStatusSubscriber",void 0),f()(this,"videoListSubscriber",void 0),f()(this,"mediaRequestSubscriber",void 0),f()(this,"playerVisibilitySubscriber",void 0),f()(this,"playbackMethodManager",void 0),f()(this,"store",void 0),f()(this,"loadContent",function(e,t,n,r){o.loadMedia(t,n,r).then(function(){o.playbackMethodManager=new rs(e)})}),f()(this,"loadMedia",function(e,t,n){var r=o.store,i=r.dispatch,a=r.getState,s=Dn.showTitle(a());if("semantic"===e){var u=pn.semanticOptions(a());return Na(u,s,n)(i)}return ka(t,s,n)(i)}),this.store=t,this.videoStatusSubscriber=new ji(t,e.getVideoStatusDependencies,this.onVideoStatusChanged.bind(this)),this.videoListSubscriber=new ji(t,e.getVideoListDependencies,this.onVideoListChanged.bind(this)),this.mediaRequestSubscriber=new ji(t,e.getMediaRequestDependencies,this.onMediaRequestChanged.bind(this)),this.playerVisibilitySubscriber=null,this.loadContent(t,r,n,i)}return Vi()(e,null,[{key:"createInstance",value:function(t,n,r,i){return new e(t,n,r,i)}}]),Vi()(e,[{key:"playNextVideo",value:function(e){var t=this.store.dispatch,n=Cn.videoList(e),r=Cn.activeVideoIndex(e)+1;n.length>1&&r>=n.length&&(r=0),r<n.length&&(!function(e){e({type:"[CORE] reset player data time params"})}(t),La(r,n[r])(t),on("play")(t))}},{key:"playPreviousVideo",value:function(e){var t=this.store.dispatch,n=Cn.videoList(e),r=Cn.activeVideoIndex(e);if(r>0){var i=r-1;La(i,n[i])(t),on("play")(t)}}},{key:"onVideoStatusChanged",value:function(e){"complete"===hn.videoTagStatus(e)&&this.playNextVideo(e)}},{key:"onVideoListChanged",value:function(e){var t=this.store.dispatch,n=Cn.videoList(e);!jn(n)&&n.length>0&&La(0,n[0])(t)}},{key:"onMediaRequestChanged",value:function(e){var t=Cn.mediaRequest(e);switch(t.type){case"playNewVideo":this.loadMedia("specific",t.value);break;case"playNextVideo":this.playNextVideo(e);break;case"playPreviousVideo":this.playPreviousVideo(e)}}}],[{key:"getVideoStatusDependencies",value:function(e){return[hn.videoTagStatus(e)]}},{key:"getVideoListDependencies",value:function(e){return[Cn.videoList(e)]}},{key:"getMediaRequestDependencies",value:function(e){return[Cn.mediaRequest(e)]}}]),e}(),os=function e(t){var n=this;Ai()(this,e),f()(this,"store",void 0),f()(this,"onDependencyFailure",function(e,t){console.log("onDependencyFailure",e,t);var r=n.store,i=r.dispatch,o=r.getState;switch(e){case"ima":"blocked"!==Fi.loadingImaStatus(o())&&Qn("error")(i);break;case"hls":er("error")(i)}}),f()(this,"onDependencyReady",function(e){var t=n.store.dispatch;switch(e){case"ima":Qn("success")(t);break;case"hls":er("success")(t)}}),this.store=t},as=function(e){return function(t){t({type:"[COMMON] set fullscreen",payload:e})}},ss=function(){function e(t,n){var r=this;Ai()(this,e),f()(this,"store",void 0),f()(this,"videoTag",void 0),f()(this,"pendingFullscreenSubscriber",void 0),f()(this,"adStatusSubscriber",void 0),f()(this,"playerUniqId",void 0),f()(this,"onAdStatusChanged",function(e){var t=_i.adStatus(e),n=r.videoTag.webkitDisplayingFullscreen;"playing"===t&&Bn()&&n&&r.exitFullscreen(r.videoTag)}),f()(this,"isPlayerInFullscreen",function(){var e=document,t=Bn()?En(r.playerUniqId):bn(r.playerUniqId);return Un(e.fullscreenElement)?!Un(e.webkitFullscreenElement)&&0===e.webkitFullscreenElement.id.localeCompare(t):0===e.fullscreenElement.id.localeCompare(t)}),f()(this,"changePlayerWidth",function(e){r.videoTag.style.width=e?"100%":"auto"}),f()(this,"onFullscreenChanged",function(){var e=r.store.dispatch,t=r.isPlayerInFullscreen();r.changePlayerWidth(t),as(t)(e)}),f()(this,"onFullscreenChangedIos",function(){var e=r.store.dispatch,t=r.videoTag.webkitDisplayingFullscreen;t||on("resume")(e),r.changePlayerWidth(t),as(t)(e)}),f()(this,"onPendingFullscreenRequestChanged",function(e){var t=gn.pendingFullscreenRequest(e);"enter"===t?r.enterFullscreen(r.videoTag):"exit"===t&&r.exitFullscreen(r.videoTag)}),f()(this,"getFullScreenElement",function(e,t){var n=document.getElementById(bn(r.playerUniqId));return Bn()?t:e?document:n}),f()(this,"enterFullscreen",function(e){var t=r.getFullScreenElement(!1,e);Bn()?t.webkitEnterFullscreen():document.webkitExitFullscreen?t.webkitRequestFullscreen():document.webkitCancelFullScreen?t.webkitRequestFullScreen():document.mozCancelFullScreen?t.mozRequestFullScreen():document.msExitFullscreen&&t.msRequestFullscreen()}),f()(this,"exitFullscreen",function(e){var t=r.getFullScreenElement(!0,e);document.webkitExitFullscreen||Bn()?t.webkitExitFullscreen():document.webkitCancelFullScreen?t.webkitCancelFullScreen():document.mozCancelFullScreen?t.mozCancelFullScreen():document.msExitFullscreen&&t.msExitFullscreen()}),this.store=t,this.videoTag=document.getElementById(En(n)),this.playerUniqId=n,document.addEventListener("fullscreenchange",this.onFullscreenChanged.bind(this)),document.addEventListener("webkitfullscreenchange",this.onFullscreenChanged.bind(this)),Bn()&&(this.videoTag.addEventListener("webkitendfullscreen",this.onFullscreenChangedIos.bind(this)),this.videoTag.addEventListener("webkitbeginfullscreen",this.onFullscreenChangedIos.bind(this))),this.pendingFullscreenSubscriber=new ji(t,e.getPendingFullscreenDependencies,this.onPendingFullscreenRequestChanged.bind(this)),this.adStatusSubscriber=new ji(t,e.getAdStatusDependencies,this.onAdStatusChanged.bind(this))}return Vi()(e,null,[{key:"createInstance",value:function(t,n){return new e(t,n)}}]),Vi()(e,null,[{key:"getPendingFullscreenDependencies",value:function(e){return[gn.pendingFullscreenRequest(e)]}},{key:"getAdStatusDependencies",value:function(e){return[_i.adStatus(e)]}}]),e}();function us(e,t){var n=Object.keys(e);if(Object.getOwnPropertySymbols){var r=Object.getOwnPropertySymbols(e);t&&(r=r.filter(function(t){return Object.getOwnPropertyDescriptor(e,t).enumerable})),n.push.apply(n,r)}return n}function cs(e){for(var t=1;t<arguments.length;t++){var n=null!=arguments[t]?arguments[t]:{};t%2?us(Object(n),!0).forEach(function(t){f()(e,t,n[t])}):Object.getOwnPropertyDescriptors?Object.defineProperties(e,Object.getOwnPropertyDescriptors(n)):us(Object(n)).forEach(function(t){Object.defineProperty(e,t,Object.getOwnPropertyDescriptor(n,t))})}return e}var ls,ds=function(e){return function(e){return e&&window.monti.playerConfigs&&window.monti.playerConfigs[e]}(e)?function(e){return window.monti.playerConfigs[e]}(e):window.monti.playerConfigs?window.monti.playerConfigs&&window.monti.playerConfigs[Object.keys(window.monti.playerConfigs)[0]]:null},ps=function e(t){var n=this;Ai()(this,e),f()(this,"videoTag",void 0),f()(this,"isBufferError",void 0),f()(this,"hls",void 0),f()(this,"hlsSetup",function(e,t,r,i){n.initiateHls(e),n.loadHlsSource(e,t,r,i)}),f()(this,"detachMedia",function(){Un(n.hls)||(n.hls.detachMedia(),n.hls.destroy(),n.hls=null)}),f()(this,"initiateHls",function(e){n.hls=new e,n.hls.attachMedia(n.videoTag)}),f()(this,"loadHlsSource",function(e,t,r,i){n.hls.on(e.Events.MEDIA_ATTACHED,function(){n.hls.loadSource(t)}),n.hls.on(e.Events.ERROR,function(t,o){n.mapHlsToErrors(e,o,i),t.details===e.ErrorDetails.BUFFER_STALLED_ERROR&&(r(!0),n.isBufferError=!0)}),n.hls.on(e.Events.FRAG_BUFFERED,function(){n.isBufferError&&(r(!1),n.isBufferError=!1)})}),f()(this,"mapHlsToErrors",function(e,t,r){if(t.fatal)switch(t.type){case 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t=hn.pendingVideoTagStatus(e),n=Dn.sources(e),i=Fi.loadingHLSStatus(e),o="blocked"===Fi.loadingImaStatus(e);r.handlePendingVideoStatus(t,n,i,o)}),f()(this,"onVideoDataChanged",function(){r.newVideoDataLoaded=!0}),f()(this,"sendPrerollPlayRequest",function(){var e=r.store.dispatch;hs("playPreroll")(e)}),f()(this,"handlePlayRequest",function(e,t,n){var i=r.store.dispatch;if(e&&e.length>0){if(r.newVideoDataLoaded&&(r.loadVideoSource(r.videoTag,e,t),r.newVideoDataLoaded=!1,r.prerollEnabled&&!n))return void r.sendPrerollPlayRequest();r.videoTag.play().catch(function(e){return console.error("Error playing the video: ",e)})}else dn(Xn.VIDEO_ERROR)(i)}),f()(this,"handlePendingVideoStatus",function(e,t,n,i){switch(e.type){case"play":r.handlePlayRequest(t,n,i);break;case"resume":r.videoTag.play().catch(function(e){return console.error("Error resuming the video: ",e)});break;case"pause":r.videoTag.pause();break;case"replay":r.videoTag.currentTime=0,r.videoTag.play().catch(function(e){return console.error("Error replaying the video: ",e)});break;case"seekTo":r.videoTag.pause(),r.videoTag.currentTime=e.value}}),f()(this,"loadMp4Source",function(e,t,n){var r=Ra(t,ys);n.setAttribute("src",r),n.load()}),f()(this,"loadVideoSource",function(e,t,n){var i=r.store.dispatch,o=Ra(t,gs);switch(fs.suitableVideoSource(e,o,n)){case"mp4":r.loadMp4Source(n,t,e);break;case"m3u8 with hls":r.videoStreamingManager.hlsLibrarySetup(e,o,function(e){return un(e)(i)},function(e){return dn(e)(i)});break;case"m3u8 directly":fs.loadHlsVideoDirectly(e,o)}}),this.store=t;var i=t.getState;this.videoStreamingManager=new fs,this.videoTag=document.getElementById(En(n)),this.prerollEnabled=bi.prerollEnabled(i()),this.pendingVideoStatusSubscriber=new ji(t,e.getPendingVideoStatusDependencies,this.onPendingVideoStatusChanged.bind(this)),this.videoDataSubscriber=new ji(t,e.getVideoDataDependencies,this.onVideoDataChanged.bind(this)),this.hlsLoadingStatusSubscriber=new ji(t,e.getHLSLoadingStatusDependencies,this.onHlsLoadingStatusChanged.bind(this))}return Vi()(e,null,[{key:"createInstance",value:function(t,n){return new e(t,n)}}]),Vi()(e,null,[{key:"getHLSLoadingStatusDependencies",value:function(e){return[Fi.loadingHLSStatus(e)]}},{key:"getPendingVideoStatusDependencies",value:function(e){return[hn.pendingVideoTagStatus(e)]}},{key:"getVideoDataDependencies",value:function(e){return[Cn.videoData(e)]}}]),e}();function ms(e,t){var n=Object.keys(e);if(Object.getOwnPropertySymbols){var r=Object.getOwnPropertySymbols(e);t&&(r=r.filter(function(t){return Object.getOwnPropertyDescriptor(e,t).enumerable})),n.push.apply(n,r)}return n}function bs(e){for(var t=1;t<arguments.length;t++){var n=null!=arguments[t]?arguments[t]:{};t%2?ms(Object(n),!0).forEach(function(t){f()(e,t,n[t])}):Object.getOwnPropertyDescriptors?Object.defineProperties(e,Object.getOwnPropertyDescriptors(n)):ms(Object(n)).forEach(function(t){Object.defineProperty(e,t,Object.getOwnPropertyDescriptor(n,t))})}return e}var Os={READY_EVENT:"ready",PLAY_EVENT:"play",PAUSE_EVENT:"pause",TIME_EVENT:"time",SEEK_EVENT:"seek",COMPLETE_EVENT:"complete",VOLUME_EVENT:"volume",MUTE_EVENT:"mute"},_s=Object.values(Os),Ss={FULLSCREEN_EVENT:"fullscreen",ANCHOR_STATUS_EVENT:"anchorStatusChanged",ANCHOR_CLOSED_EVENT:"anchorClosed"},Es={AD_PLAY_EVENT:"adPlay",AD_PAUSE_EVENT:"adPause",AD_RESUME_EVENT:"adResume",AD_COMPLETE_EVENT:"adComplete",AD_TIME_EVENT:"adTime",AD_MUTE_EVENT:"adMute",AD_SKIPPED_EVENT:"adSkipped",AD_ERROR_EVENT:"adError",AD_BLOCK_EVENT:"adBlock",AD_REQUEST_EVENT:"adRequest",AD_OPPORTUNITY_EVENT:"adOpportunity",AD_IMPRESSION_EVENT:"adImpression"},ws=Object.values(Es),Ps=Object.values(bs(bs(bs({},Os),Es),Ss)),Ts=function(){function e(t,n){var r=this;Ai()(this,e),f()(this,"eventsCallbacksHandler",void 0),f()(this,"store",void 0),f()(this,"videoStatusSubscriber",void 0),f()(this,"videoMuteSubscriber",void 0),f()(this,"videoVolumeSubscriber",void 0),f()(this,"videoTimeFragmentSubscriber",void 0),f()(this,"videoListStoreSubscriber",void 0),f()(this,"previousVideoTagStatus",void 0),f()(this,"startSeekTime",0),f()(this,"canHandleReady",function(e,t,n){if(t===Os.READY_EVENT){var r=Cn.videoList(e);if(Array.isArray(r)&&r.length>0)return n(),!0}return!1}),f()(this,"canBeHandled",function(e,t){var n=r.store.getState;return r.canHandleReady(n(),e,t)}),f()(this,"reportSeekEnd",function(e){var t={position:hn.currentVideoTimeFragment(e),offset:r.startSeekTime};r.eventsCallbacksHandler.onEvent(Os.SEEK_EVENT,t)}),f()(this,"onMuteStateChanged",function(e){var t=gn.muted(e);r.eventsCallbacksHandler.onEvent(Os.MUTE_EVENT,{state:t})}),f()(this,"onVolumeChanged",function(e){var t=gn.muted(e),n=gn.volume(e);r.eventsCallbacksHandler.onEvent(Os.VOLUME_EVENT,{level:t?0:n})}),f()(this,"onVideoTimeFragmentChanged",function(e){var t=hn.currentVideoTimeFragment(e),n=hn.currentVideoDuration(e);r.eventsCallbacksHandler.onEvent(Os.TIME_EVENT,{duration:n,position:t})}),f()(this,"onVideoListChanged",function(){r.eventsCallbacksHandler.onEvent(Os.READY_EVENT)}),this.store=t,this.eventsCallbacksHandler=n,this.videoStatusSubscriber=new ji(t,e.getVideoStatusDependencies,this.onVideoStatusChanged.bind(this)),this.videoMuteSubscriber=new ji(t,e.getVideoMuteDependencies,this.onMuteStateChanged.bind(this)),this.videoVolumeSubscriber=new ji(t,e.getVolumeDependencies,this.onVolumeChanged.bind(this)),this.videoTimeFragmentSubscriber=new ji(t,e.getVideoTimeDependencies,this.onVideoTimeFragmentChanged.bind(this)),this.videoListStoreSubscriber=new ji(t,e.getVideoListDependencies,this.onVideoListChanged.bind(this)),this.previousVideoTagStatus=hn.videoTagStatus(t.getState())}return Vi()(e,[{key:"onVideoStatusChanged",value:function(e){var t=hn.videoTagStatus(e);switch("seeking"===this.previousVideoTagStatus&&this.reportSeekEnd(e),t){case"paused":this.eventsCallbacksHandler.onEvent(Os.PAUSE_EVENT);break;case"seeking":this.startSeekTime=hn.currentVideoTimeFragment(e);break;case"complete":this.eventsCallbacksHandler.onEvent(Os.COMPLETE_EVENT);break;case"playing":this.eventsCallbacksHandler.onEvent(Os.PLAY_EVENT)}this.previousVideoTagStatus=t}}],[{key:"getVideoStatusDependencies",value:function(e){return[hn.videoTagStatus(e)]}}]),e}();f()(Ts,"getVideoMuteDependencies",function(e){return[gn.muted(e)]}),f()(Ts,"getVolumeDependencies",function(e){return[gn.volume(e)]}),f()(Ts,"getVideoTimeDependencies",function(e){return[hn.currentVideoTimeFragment(e)]}),f()(Ts,"getVideoListDependencies",function(e){return[Cn.videoList(e)]}),f()(Ts,"isContentEvent",function(e){return _s.some(function(t){return t===e})});var As=function e(t,n){var r=this;Ai()(this,e),f()(this,"eventsCallbacksHandler",void 0),f()(this,"store",void 0),f()(this,"fullscreenSubscriber",void 0),f()(this,"anchorStatusSubscriber",void 0),f()(this,"anchorDisabledByUserSubscriber",void 0),f()(this,"onFullscreenChanged",function(e){var t=gn.isFullscreenOn(e);r.eventsCallbacksHandler.onEvent(Ss.FULLSCREEN_EVENT,{state:t})}),f()(this,"onAnchorStatusChanged",function(e){var t="active"===Pr(e)?"activated":"deactivated";r.eventsCallbacksHandler.onEvent(Ss.ANCHOR_STATUS_EVENT,{state:t})}),f()(this,"onAnchorDisabledByUser",function(e){if(wr(e)){var t=hn.currentVideoTimeFragment(e);r.eventsCallbacksHandler.onEvent(Ss.ANCHOR_CLOSED_EVENT,{position:t})}}),this.store=t,this.eventsCallbacksHandler=n,this.fullscreenSubscriber=new ji(t,e.getFullscreenDependencies,this.onFullscreenChanged.bind(this)),this.anchorStatusSubscriber=new ji(t,e.getAnchorStatusDependencies,this.onAnchorStatusChanged.bind(this)),this.anchorDisabledByUserSubscriber=new ji(t,e.getAnchorDisabledByUserDependencies,this.onAnchorDisabledByUser.bind(this))};f()(As,"getFullscreenDependencies",function(e){return[gn.isFullscreenOn(e)]}),f()(As,"getAnchorStatusDependencies",function(e){return[Pr(e)]}),f()(As,"getAnchorDisabledByUserDependencies",function(e){return[wr(e)]});var Cs=function(){function e(t,n){var r=this;Ai()(this,e),f()(this,"store",void 0),f()(this,"eventsCallbacksHandler",void 0),f()(this,"adStatusSubscriber",void 0),f()(this,"adImpressionSubscriber",void 0),f()(this,"adOpportunitySubscriber",void 0),f()(this,"adTimeSubscriber",void 0),f()(this,"adMuteSubscriber",void 0),f()(this,"adProviderLoadingStatusSubscriber",void 0),f()(this,"previousAdStatus",void 0),f()(this,"canBeHandled",function(e,t){var n=r.store.getState;switch(Fi.loadingImaStatus(n())){case"loading":return!1;case"success":case"error":return!0;case"blocked":return t(),!0;case"":default:return!1}}),f()(this,"onAdStatusChanged",function(e){var t=_i.adStatus(e),n=_i.currentAdTag(e);switch(t){case"requested":r.eventsCallbacksHandler.onEvent(Es.AD_REQUEST_EVENT,{tag:n});break;case"paused":r.eventsCallbacksHandler.onEvent(Es.AD_PAUSE_EVENT,{tag:n});break;case"completed":r.eventsCallbacksHandler.onEvent(Es.AD_COMPLETE_EVENT,{tag:n});break;case"skipped":r.eventsCallbacksHandler.onEvent(Es.AD_SKIPPED_EVENT,{tag:n});break;case"playing":"paused"===r.previousAdStatus?r.eventsCallbacksHandler.onEvent(Es.AD_RESUME_EVENT,{tag:n}):r.eventsCallbacksHandler.onEvent(Es.AD_PLAY_EVENT,{tag:n});break;case"error":var i=_i.adErrorMessage(e);r.eventsCallbacksHandler.onEvent(Es.AD_ERROR_EVENT,{tag:n,message:i})}r.previousAdStatus=t}),f()(this,"onAtTimeChanged",function(e){var t=_i.adCurrentTime(e),n=_i.currentAdTag(e),i=_i.adDuration(e);r.eventsCallbacksHandler.onEvent(Es.AD_TIME_EVENT,{position:t,tag:n,duration:i})}),f()(this,"onAdMuteChanged",function(e){var t=_i.adMuted(e);r.eventsCallbacksHandler.onEvent(Es.AD_MUTE_EVENT,{state:t})}),f()(this,"onAdProviderLoadingChanged",function(e){"blocked"===Fi.loadingImaStatus(e)&&r.eventsCallbacksHandler.onEvent(Es.AD_BLOCK_EVENT)}),f()(this,"onAdImpressionChanged",function(e){var t=_i.currentAdTag(e);r.eventsCallbacksHandler.onEvent(Es.AD_IMPRESSION_EVENT,{tag:t})}),f()(this,"onAdOpportunityChanged",function(e){var t=_i.currentAdTag(e);r.eventsCallbacksHandler.onEvent(Es.AD_OPPORTUNITY_EVENT,{tag:t})}),this.store=t,this.eventsCallbacksHandler=n,this.previousAdStatus=_i.adStatus(t.getState()),this.adStatusSubscriber=new ji(t,e.getAdStatusDependencies,this.onAdStatusChanged.bind(this)),this.adTimeSubscriber=new ji(t,e.getAdTimeDependencies,this.onAtTimeChanged.bind(this)),this.adMuteSubscriber=new ji(t,e.getAdMuteDependencies,this.onAdMuteChanged.bind(this)),this.adImpressionSubscriber=new ji(t,e.getAdImpressionDependencies,this.onAdImpressionChanged.bind(this)),this.adOpportunitySubscriber=new ji(t,e.getAdOpportunitySubscriberDependencies,this.onAdOpportunityChanged.bind(this)),this.adProviderLoadingStatusSubscriber=new ji(t,e.getAdProviderLoadingDependencies,this.onAdProviderLoadingChanged.bind(this))}return Vi()(e,null,[{key:"getAdStatusDependencies",value:function(e){return[_i.adStatus(e)]}},{key:"getAdTimeDependencies",value:function(e){return[_i.adCurrentTime(e)]}},{key:"getAdMuteDependencies",value:function(e){return[_i.adMuted(e)]}},{key:"getAdProviderLoadingDependencies",value:function(e){return[Fi.loadingImaStatus(e)]}}]),e}();f()(Cs,"isAdEvent",function(e){return ws.some(function(t){return t===e})}),f()(Cs,"getAdImpressionDependencies",function(e){return[_i.adImpression(e)]}),f()(Cs,"getAdOpportunitySubscriberDependencies",function(e){return[_i.adOpportunity(e)]});var Rs=function e(t){var n=this;Ai()(this,e),f()(this,"contentEvents",void 0),f()(this,"generalEvents",void 0),f()(this,"adEvents",void 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Vi()(e,[{key:"on",value:function(e,t){this.eventsHandler.onRegisterToEvent(e,t,!1)}},{key:"once",value:function(e,t){this.eventsHandler.onRegisterToEvent(e,t,!0)}}]),e}();function Ms(e,t){var n=Object.keys(e);if(Object.getOwnPropertySymbols){var r=Object.getOwnPropertySymbols(e);t&&(r=r.filter(function(t){return Object.getOwnPropertyDescriptor(e,t).enumerable})),n.push.apply(n,r)}return n}function Is(e){for(var t=1;t<arguments.length;t++){var n=null!=arguments[t]?arguments[t]:{};t%2?Ms(Object(n),!0).forEach(function(t){f()(e,t,n[t])}):Object.getOwnPropertyDescriptors?Object.defineProperties(e,Object.getOwnPropertyDescriptors(n)):Ms(Object(n)).forEach(function(t){Object.defineProperty(e,t,Object.getOwnPropertyDescriptor(n,t))})}return e}var ks=function(){var e=window.monti.dataset;return jn(e)?(e={players:{},preact:Is(Is({},r),i),store:{},plugins:{}},window.monti.dataset=e,e):e},Ns=function(e){var t=function(){var e=(new 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os(e);Ci.getInstance().addDependenciesCallback(n)}}(n),function(e,t){ks().players[t]=new Ds(e)}(n,t),t},Ls=function(e){return console.log("player initiation start",e),new Promise(function(t,n){try{var r=function(e){var t=e.player_pos||document.currentScript.parentElement,n=e.media_id||e.content_id;return cs(cs({},e),{},{player_pos:t,media_id:n})}(function(e){var t=e.player_id,n=ds(t);return null===n?e:cs(cs({},e),n)}(e)),i=Ns(r);!function(e){var t=new CustomEvent("montiConfigLoaded",{detail:{playerKey:e}});window.dispatchEvent(t)}(i),t(i)}catch(o){console.error("Player initiation error",o),n(o)}})},xs=function(){return{initiate:Ls}};window.monti=xs,Ci.getInstance().loadExternalDependencies()}]); window.monti().initiate(Object.assign({player_pos: document.currentScript.parentElement}, {"is_conflicting_with_other_jw_players":false,"programmatic_play_with_sound_on_desktop":false,"referrer_id":"af93e181-b289-0560-a2bf-808e93bb05bc","width":"100","comscore_publisher_id":"18120612","monetization":{"ad_type":"static_tag","continue_content_play_while_waiting_for_ad":false,"strategy":"on_player_load","ad_request_timeout":"10000","midrolls":{"on":[0]},"vpaid_mode":"ENABLED","ad_tag":"https://pubads.g.doubleclick.net/gampad/ads?sz=400x300|640x480|480x270|640x360&iu=/175840252/MMPlus/smithsonianmag/Video&impl=s&gdfp_req=1&env=vp&output=vast&unviewed_position_start=1&url=##REFERRER_URL_UNESC##&description_url=##DESCRIPTION_URL_UNESC##&correlator=##CACHEBUSTER##&cust_params=mm_midroll%3D##MIDROLL_ORDER##%26video_ID%3D##VIDEO_ID##"},"sponsorship":false,"player_identifier":"mplayer","recommendation_id":null,"brand_color":"#FF9900","powered_by_strip":true,"platform":"buffy","type":"video","config_name":"MM+ | Smithsonianmag | Podding","player_id":"3v9g2u2f","playlist_id":"fSkmeWKF","playback_method":"autoplay","anchor_viewability_method":"none","player_version":"v4","playlist_type":"semantic","semantic_options":{"scan_images_on_page":true,"scanned_element":"","tags":"geogrophy,nature,animals,habitat,outdoors,science,history","minimum_date_factor":30,"scanned_element_type":"tag","scoped_keywords":"mentalfloss","promoted_videos":[]},"script_destination":"mm","publisher_contribution":"floor8","general_script_description":"","brand_logo":"","brand_logo_click_url":"","next_video":"none","uniq_key":"af93e181-b289-0560-a2bf-808e93bb05bc","content_id":"fSkmeWKF","content_type":"semantic"})); Finland has vastly improved in reading, math and science literacy over the past decade in large part because its teachers are trusted to do whatever it takes to turn young lives around. This 13-year-old, Besart Kabashi, received something akin to royal tutoring.
Kari Louhiuori, a principal at a Finnish school made a mostly unheaard of and uncanny decision to hold back an immigrant student from 6th grader named Besart because he hadnʻt felt that this young man was falling behind due to laziness but to a lack of comprehension. After a year of "royal tutoring," by allowing the boy to read at his own pace, it worked!
The work by Barros et al. looks at the role of the Ribosome Quality Control pathway (RQC) in regulating the expression of endogenous messages containing polybasic sequences. Using ribosome profiling and western blotting, the authors show that proteins containing various types of polybasic sequences are not targeted by the RQC. The authors argue that one of the few endogenous RQC substrate, RQC1, is not regulated via the canonical RQC pathway, but by a Ltn1p-dependent post transcriptional mechanism.
The question of whether there are endogenous RQC substrates has previously been explored. With the exception of the few identified substrates, such as RQC1 (Brandman et al, 2012) and SDD1 (Matsuo et al., 2020), these studies largely concluded the RQC has a minimal regulatory role for endogenous messages, and is most likely protecting cells from damage and environmental stressors. This idea is further supported by the observation that the RQC is non-essential under standard growth condition, but becomes synthetic lethal with translation inhibitors (Kostova et al, 2017, Choe et al, 2016). The work by Barros et al. comes to the same conclusions, and therefore it is unclear how this work contributes to the already established role of the RQC.
The authors also explore the regulation of RQC1 by the RQC and argue that this gene is regulated by Ltn1p in an RQC-independent way. However, mechanistic understanding of the proposed regulation is lacking, and the data are largely inconsistent with the previously published observations by Brandman et al, 2012.
Major points:
1) The authors use the dataset published by Pop et al., 2014 for their 27-29 nt no drug ribosome profiling analysis. However, these no-drug samples have been reported to exhibit surprising heterogeneity, and similarities with CHX-pretreated samples (see Hussmann et al., 2015 for detailed analysis). It is unclear how this heterogeneity can affect the analysis in the current manuscript, and whether the authors were aware of these caveats. Have the authors used independent datasets to confirm their observations? Have they excluded replicas that show CHX-like characteristics, such as A-site occupancy bias similar to CHX pretreated samples?
2) It is not clear what the purpose of the analysis presented in Fig 2 is, and how it is different from the modeling in the Park and Subramaniam 2019 paper? Are the authors using these parameters (TE, Kozak score, etc.) to show adaptations that minimize ribosome collisions?
3) Fig 3 - some of the selected examples (Dbp3, Yro2, Nop58) lack sufficient coverage in the region of interested highlighted in the right column for the short and/or long footprints. Since the data are insufficient to make conclusions about ribosome stalling and queuing, these examples should be excluded from the analysis.
4) Fig 4:
-Does ASC1 deletion cause frameshifting? Since the TAP-tag is C-terminal, it is possible that it is now out of frame, and therefore undetectable. Is it possible for the authors to introduce the tag on the N-terminus, and follow simultaneously the stalled nascent polypeptide (upon LTN1 deletion), and the full length protein?
-Is the putative stalling site of Dbp3 too close to the stat codon to cause collisions?
-Can the authors include a positive control, such as TAP-tagged Sdd1 to make sure their assay works and their strains and KOs behave as expected?
5) Fig 5:
-What is causing the inconsistency with the Brandman et al., 2012 data about RQC-dependent regulation of RQC1? In the original paper, Rqc1p has an N-terminal FLAG tag, so the authors primarily follow the stalled nascent polypeptide, whereas the current study focuses on the full length protein. Can the authors compare the same construct (FLAG-tagged Rqc1p) in their strains, so it is an "apples to apples" comparison?
-Fig 5c bottom panel - the read coverage is too sparse to make a conclusion. This analysis should be removed.
-5 d, e. The comparison between the GFP-12R-RFP stalling reporter and RQC2-TAP is not fair. The GFP construct reports on the fate of the stalled nascent polypeptide, whereas the RQC1-TAP looks at the full-length protein, and remains blind to the putative stalling product. Can the authors change the location of the tag, and repeat the experiment now looking at the stalled nascent polypeptide for RQC1? In addition, the signal in Fig. 5e look saturated. Is it possible that no effect is observed simply because the TAP signal is out of the dynamic range for the assay?
Minor Comments:
1) The introduction presents an overly simplistic view of ribosome stalling, arguing that stalling can be caused by polybasic stretches. We now know that stalling is much more complex, and there are many other factors, including the presence of non-optimal codon pairs, that cause ribosome collisions. Although the authors discuss these factors in their discussion, they should also be emphasized in the introductory paragraph.
At
Sentence structure. Most everything carries that long sentence structure. At least in the beginning parts. If it changes I will tag in the bottom when I get there!
I created a pull request to have the if (node.parentNode) conditional added to detach. It was not applied due to the desire to find the root cause of the <meta> tag manifestation of this issue.
Bug repro for https://github.com/sveltejs/svelte/issues/2086
Fixed by: Bug 1:
Bug 2:
Fixed version here: https://svelte.dev/repl/a55ba18ceca44c898f2b011a0978de85?version=3.6.7
(although https://github.com/sveltejs/svelte/pull/3172/commits/f4ca063c85e491b75d162f429ad243b6f443db13 indicates the fix was included in v3.6.6 tag, so I wonder why it's not fixed here)
supersedes https://codesandbox.io/s/epic-stonebraker-9cxhu?file=/index.js:0-32
Good example of how helpful it is to remove everything irrelevant and create minimal reproducible example.
Canadian government at the end of 2020
about what i 1der.
The FBI said it has stopped using the "Black Identity Extremist" tag and acknowledged that white supremacist violence is the biggest terrorist threat this country faces.
When using the "Always Check" Approach, this headline generated many relevant Google searches, with multiple other media outlets covering this. Hence, The Root appears to be credible. I'm very surprised that it took a long time for the FBI to make this decision.
setContext must be called synchronously during component initialization. That is, from the root of the <script> tag
The <output> tag represents the result of a calculation. Typically this element defines a region that will be used to display text output from some calculation.
How <output> tag can be used in HTML5
D&D is the superior mental health resource
Useful tag with stories and experiences
globals are assumed to have their field value on the window object and can be referenced inside the bundle by their field name globals: { name: 'Value', }, assumes that some other script tag or whatever establishes window.Value and the emitted umd bundle for example, calls the factory like factory(global.Value). So globals is just stuff to bring into the factory on the globals object. It doesn't even make it "global" inside the bundle. Basically, the resolver does not check the globals object during the loading process. The resolver needs to be told how to link these globals and that's what the external option is for. external: ['name'], Then you can reference it like import myName from 'name'; myName();
Previous work has shown that the nuclear import of TyrRS is stimulated under stress and that nucleus-localized TyrRS functions through the transcriptional machinery to promote the expression of DNA damage response genes for cell protection. In this work, evidence is presented that nuclear TyrRS also inhibits bulk translation in a manner correlated with its association with several AARS-encoding genes and that for elongation factor eEF1A, and recruitment to these genes of HDACs. Mutation of the TyrRS NLS, whose function in nuclear localization provides for coupling between low tRNATyr binding and nuclear localization, was found to derepress bulk translation after prolonged oxidative stress by H2O2, without altering eIF2 phosphorylation levels or mTOR activation, and overexpression (o/e) of TyrRS can reduce protein synthesis, in a manner enhanced by the E196K mutation associated with Charcot-Marie-Tooth disease (CMT), shown previously to enhance TyrRS association with transcriptional co-repressors. ChIP-Seq of overexpressed V5-tagged TyrRS showed binding to only 17 sites, of which 15 are within gene coding sequences, among which four encode TyrRS, TrpRS, SerRS and GlyRS, and a fifth encodes elongation factor eEF1A. These results were confirmed by ChIP analysis of endogenous TyrRS, using the HisRS gene as negative control; and the occupancies were shown to increase on H2O2 treatment. The expression of these AARS/eEF1A gene transcripts was shown to be reduced by o/e of TyrRS, in a manner enhanced for at least some of them by the E196K CMT mutation; and the repression was shown to be eliminated by the NLS_mut for YARS expressed at native levels. Reductions in AARS/eEF1A protein expression were also observed on WT TyrRS o/e. Sequence analysis of the genes showing TyrRS binding by ChIP-seq led to identification of a motif that was shown to be required for binding to TyrRS in vitro in EMSA assays with either purified TyrRS or in extracts from cells overexpressing it, in a manner requiring the full-length TyrRS and not only the catalytic core of the enzyme. It was not shown however that eliminating this motif from any of the target genes attenuated their repression by nuclear-localized TyrRS. Mass spec analysis of affinity-purified, overexpressed TyrRS identified interacting proteins, and several of which were shown to be coimmunoprecipitated with endogenous TyrRS in non-stressed cells, including the transcription cofactors Trim28, HDAC1, and subunits of the NURD co-repressor/histone deacetylase complex. ChIP assays showed that overexpression of TyrRS lead to decreased levels of H3K27Ac, a histone mark of active transcription, and elevated occupancies HDAC1, TRIM28, or NURD subunit CHD4 in non-stressed cells at the AARS/eEF1A genes, with either TRIM28/HDAC1 or CHD4 being observed for all of the genes except the TyrRS gene that shows all three cofactors present. Based on these results, the authors conclude that increased nuclear localization of TyrRS on oxidative stress leads to increased binding of TyrRS to the AARS/eEF1A genes with attendant direct recruitment of either TRM28/HDAC1 or NURD, leading to transcriptional repression of these genes, which is responsible for the reduction in bulk protein synthesis observed after prolonged H2O2 treatment. They go on to provide evidence that cell survival in H2O2 is enhanced by nuclear association of TyrRS (dependent on the NLS), and that in its absence, conferred by the NLS_mut, apoptosis is increased. They also show that ROS increases by preventing TyrRS nuclear localization by the NLS_mut, and that this effect as well as decreased cell survival for this mutant in H2O2 can be rescued by the translation elongation inhibitor harringtonine.
The results presented in this report provide some support for the main conclusions of the paper and the overall model presented in Fig. 4F. However, as detailed below, many of the main conclusions of the paper are based on correlations and lack direct experimental support, and a number of the experiments are not comprehensive enough with sufficient conditions and controls to establish that the effects observed can be attributed to enhanced nuclear localization of TyrRS in response to H2O2. Considering the statements in the abstract, the evidence is reasonably strong that nuclear localization of TyrRS leads to inhibition of global translation at a stage later than that of eIF2α/ATF4 and mTOR responses, and that excluding TyrRS from the nucleus increases apoptosis under prolonged oxidative stress (although even this last point requires better documentation). However, the evidence is inadequate in several respects to claim that TyrRS directly represses the transcription of translation-related genes by recruiting TRIM28 or NURD complex, and as claimed on p. 13 of the Discussion, that the repression of the four AARS genes and the gene for eEF1A accounts for the reduction in bulk protein synthesis on H2O2 treatment.
Major issues:
-Evidence is lacking that the binding of TyrRS to the AARS/eEF1A genes is functionally important for the repression of any of the 6 putative target genes upon increased nuclear localization of TyrRS conferred by the NLS_mut or in response to H2O2. This would require ChIP analysis of TyrRS binding to the target genes for WT vs. NLS_mut TyrRS in H2O2-treated cells; and CRISPR mutagenesis of the putative TryRS binding site in the genome and analysis of transcription in the presence and absence of H2O2 for at least one of the putative TyrRS target genes.
-Evidence from ChIP analysis is lacking that TRIM28, HDAC1, or the NURD complex are recruited to the AARS/eEF1A genes at native levels of TyrRS in a manner dependent on the NLS and stimulated by H2O2, as the ChIP experiments involved only overexpressed WT TyrRS in non-stressed cells. It is also unclear whether H3K27Ac levels at the putative target genes decline at endogenous levels of TyrRS on treatment with H2O2. Similarly, evidence is lacking that the physical association of TyrRS with these co-repressors is dependent on the NLS and stimulated by H2O2, as the co-IP analysis was limited to endogenous WT TyrRS in non-stressed cells.
-Evidence is lacking that the cofactors TRIM28, HDAC1, or CHD4 are required for the down-regulation of target gene transcription on H2O2 treatment, which would require knock-down or elimination of these factors by CRISPR accompanied by analysis of target gene transcription +/- H2O2.
-Direct evidence is lacking from ChIP analysis of RNA Pol II that the transcription of the AARS/eEF1A genes is reduced on H2O2.
-Evidence is lacking that the repression of bulk protein synthesis is actually mediated by the reduced expression of the 4 AARSs and eEF1A. The fact that the TyrRS-E196K mutation enhances repression of bulk translation and also repression of 3 of the 5 target genes does support the idea that the repression of the target genes is instrumental in reducing protein synthesis, but again, this is still a correlation. There is no evidence that the reduced expression of the AARSs is sufficient to reduce charging of the cognate tRNAs, or that the reduced expression of eEF1A decreases the rate of translation elongation in cells or cell extracts.
-There is an important lack of information provided needed to evaluate the quality and significance of the ChIP-seq analysis of TyrRS binding to DNA. No details are provided concerning the ChIP-seq analysis of V5-tagged TyrRS to indicate how the TyrRS occupancy peaks were identified and distinguished above background signal from the cells expressing V5 tag alone, whether replicates were examined to provide statistical significance for the identified occupancy peaks, and the sequencing library depths. No genome browser views were provided to show the signals from the cells expressing V5-TyrRS vs V5 alone to demonstrate the quality and reproducibility of data from replicates. The supplementary table S1 describing these data was even omitted from the submission, and it's unclear whether these data are being deposited in GEO.
-There is an important lack of information provided needed to evaluate the quality and significance of the mass-spec analysis of TyrRS interacting proteins. No details are provided about the statistical significance of the protein interactions identified by mass-spec analysis of the affinity-purified TyrRS; and a negative control for non-specific association seems not to have been included in the analysis. The supplementary table describing these data was even omitted from the submission.
-It's unclear whether the motif described in Fig. 3A was found under the peaks of TyrRS occupancy in the various genes showing TyrRS binding in the ChIP-seq experiments, nor whether its occurrence is statistically significant. It was not indicated that the motif coincides with the peak ChIP-seq occupancies for TyrRS, and if not, how this could be explained.
-Evidence is lacking that harringtonine treatment reduced bulk protein synthesis under the conditions where it suppressed the effects of the TryRS NLS mutation in elevating ROS and decreasing cell survival.
-In general, the figure legends are poorly written in lacking important details about the nature of the TyrRS being examined in the experiment (tagged vs endogenous; overexpressed vs. native levels), and also whether oxidative stress was imposed in the experiment, and if so, the exact conditions for the treatment. Figure legends should contain all of the critical details needed to understand and evaluate the significance of the experimental results without having to search elsewhere in the paper for them.
-It needs to be clarified whether the mini-TyrRS construct lacks the NLS, and the significance of its behavior as a negative control for the effects of overexpressing WT TyrRS.
-For the experiment in Fig. 5B, quantification of the fraction of caspase-3 or PARP cleaved from biological replicates is required.
-The experiment in Supp. Fig. S4 lacks the results from cells untreated with H2O2 to ensure that these proteins were being induced by H2O2 in their hands.
including computer vision, machine vision, speech recognition, natural language processing, audio recognition, social network filtering, machine translation, bioinformatics, drug design, medical image analysis, material inspection and board game programs, where they have produced results comparable to and in some cases surpassing human expert performance<br> yes ma
yes mam
private and public both
hi mam
Your tooltip component will have to wrap your image with a span tag or something, it can’t just add events to its children. And if you are adding multiple actions to it you will have to wrap it multiple times.
vs.
<img use:concern1 use:concern2>
No, this is about using a string to create an element of that tag name.
{#each section as {tag, is_self_closing, props, content}} {#if is_self_closing} <{tag} {...props} /> {:else} <{tag} {...props}>{content}</{tag}> {/if}
“Who are you then?" "I am part of that power which eternally wills evil and eternally works good.”
Anti‐Flag monoclonal
DOI: 10.1096/fj.202001340R
Resource: (Wako Cat# 018-22381, RRID:AB_10659453)
Curator: @Naa003
SciCrunch record: RRID:AB_10659453
Curator comments: Anti-DYKDDDDK tag Monoclonal Antibody, Unconjugated, Clone 1E6 Wako Cat# 018-22381
anti‐Myc‐tag
DOI: 10.1096/fj.202001340R
Resource: (MBL International Cat# 562, RRID:AB_591105)
Curator: @Naa003
SciCrunch record: RRID:AB_591105
Curator comments: Rabbit Anti-Myc Tag Antibody, Unconjugated MBL International Cat# 562
Thompson, Hoping for More.
Thompson, Deanna A.; 166 pp. $19 from Amazon; $10 Kindle.
kit/biblioteca_soñada
Ich würde das, was du hier diagnostizierst, als Epistemic Crisis bezeichnen. Ich nehme sie genauso wahr wie du, und ich bin auch darüber entsetzt. Das erste Warnsignal, das ich ernst genommen habe, war der Brexit, das zweite die Wahl von Trump. Beide habe ich vorher nicht erwartet, weil sie jenseits des Horizonts waren, in dem ich Entwicklungen erwartet habe. ich muss also auch an der Art und Weise zweifeln, in der ich politische Entwicklungen verstanden habe.—Später kam dann für mich der Aufstieg der Freiheitlichen hier in Österreich, bis hin zur Regierungsbeteiligung, und die rechtspopulistische Welle (wenn man es so nennen will) in Frankreich und Italien.
Your solution is a very basic. The case above is more complex because using your solution you can't manipulate with fetched data outside of template and even outside {#await / } tag. So, if you need a read-only solution it's good but otherwise, it won't help you.
I save the things I read online, too, in a digital research library. I’ve long used Evernote to clip the full text of articles I find and gather them in various digital notebooks, separated into categories for easy reference. I can full-text search everything that I've saved over the past decade, to find the citation really quickly. The combination of my physical library and my note-taking softwares act as a kind of external brain—in other words, my memory gets me to the original source of what I’ve read by searching my notebooks, Evernote, or Pinboard.Recently I’ve been migrating this clip-taking to Pinboard, inspired by a Superorganizers post. Pinboard is much like Evernote, but allows you to tag clipped articles into multiple categories. Pinboard automatically saves a full-text version of each page you clip, so you can search and reference the text even if the website is removed or the page is no longer available.
Pinboard, huh? I should take a look at this.
The RFID tag - short for Radio-Frequency Identification - is ubiquitous in the modern economy.
Bugs
Say I want to style this javascript routing anchor tag on various pages (some may be buttons, plain links, images) it makes it incredibly difficult. Eg:
learning
In your initial tag line you have "education" and I like that better. It is just a bit more broad.
Reviewer #1:
Major comments:
1) The title and the conclusion that SON and SRRM2 form nuclear speckles are not supported by the data. The data show that SON and SRRM2 are necessary for nuclear speckle formation. They do not rule out that another factor is necessary, such as SRRM1, which interacts with SRRM2 and itself harbors an intrinsically-disordered domain. That is, the authors have not shown that SON and SRRM2 are also sufficient for nuclear speckle formation. Such a test is necessary to draw the strong conclusion the authors make, and precedence for such a test has been established in the study of Cajal bodies. Specifically, central factors to Cajal body formation were shown to nucleate Cajal body formation at a specific site in chromatin when such central factors were localized to that site. The authors either need to perform such a sufficiency experiment or moderate their conclusions (and title).
2) In principle, in the immunofluorescence studies, the disappearance of mAb SC35 signal on depletion of SRRM2 does not alone prove that SRRM2 is what is visualized by the mAb SC35 in such assays. Given that this paper seeks to establish rigorously that mAb SC35 marks nuclear speckles by recognition of SRRM2, given that SRSF7 is recognized by the antibody on blots, and given that SRSF2 has been traditionally presumed the target of mAb SC35 in nuclear speckles, the rigor of this study demands that SRFS7 and SRSF2 be visualized in cells in the presence of an SRRM2 truncation to rule out that either SRSF7 or SRSF2 phenocopy SRRM2 in this assay.
This is a valid concern and we have thought of the same principal that is if any strongly speckle-associated intrinsically disordered domain containing protein, such as SRRM1 or RBM25, two proteins that are also frequently used as NS markes, would have a similar impact on NS formation as SRRM2 has. To this end, we performed a co-depletion of SON and SRRM1 (shown in Supplementary Figure 10) in a cell line that has a TagGFP2 inserted into SRRM2 gene locus. As it can be seen from the imaging presented in this figure for 4 individual cells (but also more generally on 10 independent field imaged, (data not shown)) we did not score a reduction in the GFP intensity, or dissolution of the spherical bodies as is the case in SON-SRRM2 co-depleted cells. We observed the nuclear speckles have the round-up morphology, that is seen upon SON-KD, but are not dissolved shown with PNN staining and SRRM2-TagGFP signals. Moreover, we performed a co-depletion of RBM25 (another strongly NS-associated protein also used as a NS-marker) and SON which did not result in the dissolution of nuclear speckles (Supplementary Figure 10). Therefore, we have reached to the conclusion that SON and SRRM2 form nuclear speckles with the contribution of SON being more important for the formation and titled our study accordingly.
Traditionally, because of the Fu & Maniatis 1992 paper, as pointed out by the reviewer, it is assumed that SC-35 recognizes SRSF2 in immunofluorescence experiments and potentially multiple SR-proteins in immunoblots. The former point, to the best of our knowledge, has never really been proven in any type of rigorous experiment. Fu lab. has generated SRSF2 K/O mice, but never provided an immunofluorescence image that shows that SC-35 signal disappears in K/O cells.
Just to summarize our line of reasoning here:
1) We do an unbiased IP-MS experiment, which shows that SRRM2 is the top candidate protein, at least an order of magnitude away from any other protein in the dataset by any measure. This strongly suggest that SRRM2 is the primary target of this antibody, although doesn’t prove it due to technical reasons i.e. no input normalization, some proteins produce more ‘mass-specable’ peptides than others, and larger proteins tend to produce more peptides.
2) We carry out a biased screen of 12 SR-proteins and find that SRSF7 is strongly recognized by mAb SC-35
3) We do IP-western blotting experiments, which correct for input and are not affected by relative ‘mass-specable’ peptide issues or protein sizes, which reveal a strong enrichment of SRRM2 (>10% of input), some enrichment for SRSF7 (~2% of input) and no enrichment for SRSF2, SRSF1 or other proteins that we have tested.
4) Since the “35kDa” protein is so engrained with the history of this antibody and our results were most consistent with the idea that this protein is SRSF7 rather than anything else, we insert a degron tag to SRSF7. If the hypothesis is true, then we expect a shift of the SC-35 band, concomitant to the shift in SRSF7, which is indeed the case. This is not proof that SC-35 doesn’t recognize any other protein but it does provide very strong evidence (combined with the other two experiments) that the 35kDa band detected by SC-35 in immunoblots is in fact SRSF7.
5) We then show, by TagGFP2 insertion into the SRRM2 locus, that SC-35 mAb can recognize SRRM2 specifically on immunoblots, and furthermore truncations beyond a certain point completely eliminates this signal. We also show later that siRNA mediated KD of SRRM2 also leads to the elimination of the signal from immunoblots (Supplementary Figure 9).
6) Combining the results so far, we address the issue of immunofluorescence, i.e. which protein or proteins are responsible for this signal. We think there are two possible scenarios that could both be true based on the presented evidence so far:
a. This signal is mainly, if not entirely, originates from SRRM2. b. The signal is a combination of SRRM2, SRSF7 and/or other SR-proteins that the SC-35 might be cross-reacting.
7) We then take advantage of our cell lines with SRRM2 truncations. These truncated SRRM2 version are not recognized by SC-35 mAb on immunoblots, therefore it is reasonable to suspect that they will not be recognized by SC-35 mAb in immunofluorescence as well.
8) If scenario (b) is correct and nuclear speckles are still intact in these cells (which we show that they are indeed intact, judged by SON, RBM25 and SRRM1 stainings Fig. 3A-B), then we would expect either no change in SC-35 signal, or a somewhat reduced signal. We see a complete loss of signal.
9) Being extra careful with this result, we also mix the control cell line and SRRM2-truncated cells and image them side-by-side to address any issues related to imaging settings etc. There is no detectable SC-35 signal in truncated cells.
10) We also show that the 35kDa band is still unchanged in SRRM2 truncated cells (Figure 2E), showing that SRSF7 itself is not affected in these cells.
These results, combined together, show that SC-35 signal in immunofluorescence originates from SRRM2, and any other signal potentially contributed by other proteins are below the detection of immunofluorescence microscopy.
Reviewer #2:
This study reports important evidence that the widely-used SC-35 antibody primarily recognizes SRRM2 rather than the assumed SRSF2. The manuscript provides several lines of evidence supporting this conclusion, and the work has broad impact on the field of nuclear structure and function as this antibody is the most common marker for the major nuclear component, nuclear speckles.
The one concern with the manuscript is the interpretation of some of the previous literature and understanding in the field.
First, since the 1990s it has been widely known that the SC-35 mAb has very limited specificity for denatured proteins and was not suitable for immunoblots (see abcam page for ab11826). Indeed, the assumption has always been that it recognizes a folded epitope. Therefore, the use of western blots to conclude anything about the specificity of this antibody is inappropriate.
Secondly, it has also been previously documented that this antibody has cross-reactivity with SRSF7 (i.e. 9G8; Lynch and Maniatis Genes Dev 1996).
Third, most SR proteins are not abundantly observed in tryptic MS due to high cleavage of RS domains. This is particularly true of SRSF2, which has a highly "pure" RS domain (i.e. all RS repeats) that encompasses almost half of the total protein. SRRM2, on the other hand, has much more complex and degenerate RS domains that encompass a much smaller percentage of the total protein. SRRM2 is also 10x the size of SRSF2. Thus, given equal molar amounts of SRSF2 and SRRM2, one would expect at least 20x the number of peptides and much more complete coverage of SRRM2 vs. SRSF2. Therefore, while the subsequent immunoblot in Figure 1C is compelling evidence that SRRM2 is precipitated with the SC-35 antibody, while SRSF2 is not, the IP-MS data alone is not strong proof that the SC35 mAb primarily recognizes SRRM2 rather than SRSF2. The text should be revised accordingly.
Finally, the abstract implies that the demonstration of SON as a central component of speckles is new ("elusive core"). As appropriately referenced in the text, this is not the case, rather SON is often used as a marker for nuclear speckles, and SON has long been considered to be part of the core of speckles, as knock-down has been documented by several groups to disrupt speckles. The wording in the abstract should therefore be more parsimonious.
With all due respect to all previous researchers that have used mAb SC35 and published their results, we think that the specificity issue has become unnecessarily convoluted due to the initial inaccurate characterization. Abcam’s recommendations highlight the issue in an interesting way. In the old marketing images, abcam shows a single band in a total lysate prepared from HEK293 cells: https://www.abcam.com/ps/products/11/ab11826/reviews/images/ab11826_49518.jpg
However, producing such an image, in our experience as we have also reported in the manuscript, is only possible under non-ideal western-blotting conditions i.e. when the transfer is not adequate to reveal proteins with large molecular weights. Intriguingly, a customer (not us) complains about an improper WB result obtained with this antibody (with a 2-star rating):
It looks like an unexplainable high-molecular smear without the information that we provide in our manuscript, but in light of it, it’s clear that protein stained here is SRRM2.
In our experience the antibody works perfectly fine for western blotting, and very specifically and robustly reveals SRRM2 at ~300kDa, as long as the immunoblotting conditions are optimized for large proteins. We also show that bulk of the signal around 35kDa originates from SRSF7, however as indicated by the other reviewer’s comments, and also previous research, the antibody probably cross-reacts with other proteins as well with varying degree.
In this sense, the antibody can be used for immunoblotting, but pretty much any result obtained from such an experiment must be verified with an independent antibody or independent methods, which we did in this manuscript.
The SC35 mAb is actually suitable for western blotting if the gel running and transfer conditions are carefully performed to have SRRM2: a) enter the gel and b) transferred properly to the membrane. Under conditions where SRRM2 is just not entering the gel (due to high percentage gels, or gels with too much bis-acrylamide), or doesn’t get transferred to a membrane (non-ideal buffer conditions, protein stuck in stacking part and cut away etc.), we have seen the unspecific bands, but we had to use the most sensitive detection reagents at hand to see those, so they are rather weak. We have provided a detailed explanation to what these conditions are in the methods section of our manuscript, but briefly: running the gel slowly allowing the protein to enter in the gel and transferring overnight with CAPS buffer were key to get the western blot working. As we have shown in Figure 2C and 2E, the majority of signal detected comes from SRRM2. The unspecific binding of SC35 mAb could only be scored if the above-mentioned conditions were not met.
We believe what made matters historically worse has been the use Mg++ precipitation that enriches many SR proteins, but actually completely depletes SRRM2 (Blencowe et al. 1994 DOI: 10.1083/jcb.127.3.593, Figure 5, https://pubmed.ncbi.nlm.nih.gov/7962048/ ). When we’re sure that SRRM2 is in the gel though, it just shines as a single band. So in conclusion, SC-35 is reasonably specific to SRRM2, especially in immunofluorescence, but it certainly cross-reacts with other SR-proteins, especially when SRRM2 is missing for technical or biochemical reasons.
We will update in the manuscript for the corresponding section by citing earlier studies reporting the specificity issues of mAb SC35.
We absolutely agree that IP-MS data alone is not enough to conclude that SC-35 recognizes SRRM2, or whether it is the primary target or not. The overwhelming amount of SRRM2 peptides detected, in addition to the overwhelming amount of total peptide counts from SRRM2 does strongly suggest that it is the case, which we then followed up by IP-western blotting which controls for relative input, and the various experiments shown in later figures.
We have looked at our MS results and found out that:
SRSF2 was detected with 4 unique peptides with an MS/MS count of 5 and a sequence coverage of 29% (intensity 3E+07), whereas SRRM2 was detected with 227 unique peptides with an MS/MS count of 3317 and a sequence coverage of 61.9% (intensity 2E+11).
These numbers show a 6600 times higher intensity for SRRM2 (not normalized). As the identification and abundance of different peptides/proteins can by dramatically different in MS, it is indeed correct that one should be careful with such comparisons. The only way would be to use peptide standards for both proteins and record standard curves, then a real quantitative comparison would give the true numbers. Hence, we will revise the wording of that section.
Finally, as the reviewer has pointed out, we have not shown that speckles can be reformed by introducing ectopically expressed SON/SRRM2 into cells which now appear not to have nuclear speckles. This would indeed be the formal proof showing that SON/SRRM2 are not just necessary but also sufficient to form nuclear speckles. Such an experiment is quite challenging due to the length of these proteins and difficulty in establishing conditions where one can express these proteins, but not overexpress them which leads to round-up speckles (as shown and discussed by Belmonte lab). Therefore, we will change the title to “SON and SRRM2 are essential for the formation of nuclear speckles” to better reflect our conclusions.
We really did try to be clear and just about the previous literature around SON. Indeed, it is clear that SON is a crucial part of NS, likely the most important component for the integrity of speckles. However, in all of these previous studies, RNAi-mediated depletion of SON, without exception, leaves behind spherical bodies that are strongly stained with mAb SC35, that also harbor other NS-markers (which we also show). This is of course not new, as we also appropriately cited previous work, however being able to dissolve these “left-over” speckles by co-depletion of SRRM2, and perhaps more importantly by deletion of the SRRM2’s C-terminal region is indeed novel.
In essence, our results show that in the absence of SON, as shown by previous work as well, NS-associated proteins are still able to organize themselves into nuclear bodies, indicating that either all other SR-proteins without the need of another organizer clump together, or another factor (or factors) is still acting as an organizer. When we remove the C-terminus of SRRM2, which we show is the primary target of SC-35, which strongly stains these left-over nuclear bodies in the absence of SON, then deplete SON, all NS markers that we could find become diffuse, indicating that nuclear speckles no longer exist, or become too small to be detected or classified as “nuclear bodies”. Co-depletion of SON and SRRM2 leads to the same phenotype, but co-depletion of SON and SRRM1 (or RBM25) doesn’t, leaving behind spherical nuclear speckles that harbor SRRM2 which are no different than SON KD cells.
Reviewer #3:
Nuclear speckles in the last several years have attracted significant attention for their association with transcriptionally active chromosome regions (after largely being ignored by most for the previous 20 years). Overwhelmingly, a single monoclonal antibody has been used as a marker for nuclear speckles for several decades.
This manuscript now argues convincingly that the main target that is recognized by this monoclonal antibody is not SRSF2 (SC35) as long thought, but rather SRRM2. The authors thus clarify a vast literature, while also focusing attention on the very large protein SRRM2 that in many ways resembles another nuclear speckle protein, SON. Both have huge IDRs and unusual RS repeats, while SON has been proposed to act as a scaffold for many SR-containing proteins, which is likely also true for SRRM2, by extension. Moreover, the manuscript provides a convincing explanation for why the target of this antibody was previously misidentified, by showing a lesser cross-reaction with SRSF7, of similar MW to SC35.
Finally, the manuscript suggests that SON and SRRM2 together help nucleate nuclear speckles, as a double KD, or a SON KD in a background of a truncated SRRM2, leads to loss of nuclear speckle-like staining of other proteins normally enriched in nuclear speckles (RBM25, SRRM1, PNN). The authors go on to suggest that this double KD approach will now provide an important means of disrupting nuclear speckles to aid in functional studies.
Interestingly, some of the results of this manuscript actually are already confirmed or consistent with previous literature. For example, a cited paper describes changes in Hi-C compartmentalization patterns after "elimination" of nuclear speckles- actually, they performed a SRRM2 KD and showed loss of SC35 staining, which is now explained as simply due to the KD that they performed. More recently, a new proteomics study of nuclear speckles (Dopie et al, JCB, 2020: https://doi.org/10.1083/jcb.201910207) reported both SON and SRRM2 as the two most highly enriched nuclear speckle proteins, with enrichment scores similar to each other but more than twice that of all other speckle proteins. Moreover, this same paper also did a SRRM2 KD and observed loss of anti-SC35 staining but not SON staining.
Overall, I found this manuscript of significant interest for people in the nuclear cell biology field and technically thorough and well done. I just had one issue and one point to make in my main comments, plus some minor points.
1) The evidence that nuclear speckles are nucleated by SON and SRRM2 is based on the dispersion of staining of nuclear speckle proteins RMB25, SRRM1, and PNN. However, an alternative explanation is that some other protein(s) nucleates nuclear speckles, while these other nuclear speckle proteins bind to SON and SRRM2, and are therefore enriched in nuclear speckles. To eliminate this concern, the authors could show that SON and/or SRRM2 do not bind to these proteins- for instance using co-IP or other methods. Of course, it could be that such binding or scaffolding of nuclear speckle proteins is how they form nuclear speckles. But just one protein that is not bound by SON and SRRM2 but still stains nuclear speckles after the double KD would be inconsistent with their hypothesis. Therefore, if they do find that all these proteins bind SON and/or SRRM2 they could simply discuss this as a scaffolding mechanism but qualify their conclusion based on the alternative explanation described above.
2) In our lab we have not been comfortable using the kinase manipulations, discussed in this paper, to eliminate nuclear speckles for experimental purposes because the cells appear very sick after these manipulations. For other reasons, we also tried a double SON and SRRM2 KD. Our experience is that the cells after this double KD were also not very normal. If the authors are suggesting the SON and SRRM2 double KD as an experimental tool to disrupt nuclear speckles in order to access nuclear speckle function, then it would be valuable for them to indicate cell toxicity, etc. Many SR-protein KDs for example do not allow selection of stable cells. What about this double KD?
The first point of Reviewer #3 has been addressed above in response to the Reviewer #2.
We have stated that our work identifying SON and SRRM2 as the elusive core of nuclear speckles paves the way to study the nuclear speckles under physiological conditions. Here, we have used the cells 24 hours after transfection (~18 hours of knock-down) as the primary reason being that SON-KD caused a mitotic arrest if the cells were kept longer in culture. This was reported earlier in Sharma et al MBC 2010. There was no additional severity in the phenotype when the SON-KD was combined with SRRM2-KD, therefore we believe the arrest phenotype we scored is mainly due to depletion SON. In this sense, double-depletion of SON and SRRM2 can be used to study the effects of loss of NS (transcription, post-transcriptional, topological), but certainly within a time-frame of around 24 hours in cells that haven’t gone through mitosis. We will clarify this statement in the revised manuscript to avoid any misunderstanding as pointed by the reviewer. Faster depletion strategies, and/or a system where cells are mitotically arrested would be required to observe long term effects more reliably.
This package exposes an hyperscript compatible function: h(tag, properties, ...children) which returns a svelte component.
Mouse anti-HA
DOI: 10.1016/j.celrep.2020.108101
Resource: AB_2864345
Curator: @Naa003
SciCrunch record: RRID:AB_2864345
Curator comments: HA-Tag (26D11) Mouse Antibody Abmart Cat# M20003
.h1 test
this is a .tag-test
To add documentation on a Svelte component that will show up as a docstring in LSP-compatible editors, you can use an HTML comment with the @component tag:
n the Iranian case, meanwhile, the people tweeting about the demonstrations were almost all in the West. “It is time toget Twitter’s role in the events in Iran right,” Golnaz Esfandiari wrote, this past summer, in Foreign Policy. “Simply put: There wasno Twitter Revolution inside Iran.” The cadre of prominent bloggers, like Andrew Sullivan, who championed the role of socialmedia in Iran, Esfandiari continued, misunderstood the situation. “Western journalists who couldn’t reach—or didn’t botherreaching?—people on the ground in Iran simply scrolled through the English-language tweets post with tag #iranelection,” shewrote. “Through it all, no one seemed to wonder why people trying to coordinate protests in Iran would be writing in anylanguage other than Farsi.”
twitter protesters forget to translate text about votings in Iran and were inconsiderate to the fact that they speak farsi there. they are protesting without actually aiming to create change.
In the Iranian case, meanwhile, the people tweeting about the demonstrations were almost all in the West. “It is time to get Twitter’s role in the events in Iran right,” Golnaz Esfandiari wrote, this past summer, inForeign Policy.“Simply put: There was no Twitter Revolution inside Iran.” The cadre of prominent bloggers, like Andrew Sullivan, who championed the role of social media in Iran, Esfandiari continued, misunderstood the situation. “Western journalists whocouldn’t reach—or didn’t bother reaching?—people on the ground in Iran simply scrolled through the English-language tweets post with tag #iranelection,” she wrote. “Through it all, no one seemed to wonder why people trying to coordinate protests in Iran would be writing in any language other than Farsi.”
western journalists took matter into their own hands without truly knowing what was happening from people inside of Iran. they took what they knew from things they collected from twitter and put it into their own hands. this is where i strongly disagree with social media activism. you may not need to be face to face but you do need to speak directly to people instead of making assumptions.
Ein Tag im Exilwo die Stunden sich bückenum aus dem Keller ins Zimmer zu komme
Die Verkorperung hier ist sehr stark und ich finde das sehr interessant, dass Auslander eine Person, die aus dem Keller kommt, mit die Stunden in Exil. Ich glaube, dass die Stunded durch einen Tag sich andern. Was meint ihr, was die Wirkung von die Verkorperung hier ist?
Ein Tag im ExilHaus ohne Türen und FensterAuf weißerTafel mit Kohle verzeichnetdie Zeit
Die Exilerfahrung wird hier wie eine Haftstrafe beschreibt. Was ist die Wirkung von diesem Vergleich?
roughly $500 billion
Wow thats a large price tag.
「晨间记录」和「晚间思考」（Morning Journal & Evening Reflectin）这两个板块用于早晚的个人记录和总结。「输入（Input）」指我这一天做了什么、学了什么、了解了什么；「输出（Output）」则更关注产出，包括「地标（Landmark）」这样值得铭记的成就和阶段性成果；「个人观察记录」更多是跟我身心状态相关的记录。如果我工作在一个具体而较为宏观的任务上，我就会选择创建对应 Page 并跳转到其中去工作。等待任务完成再回到 Journal 中。此外，如果不生成新页面的话，我会尽量给某个记录添加相应的 Tag，以便索引。
rabbit anti-HA epitope tag, DyLight™ 549
DOI: 10.1186/s13064-020-00146-6
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Curator comments: Anti-HA EPITOPE TAG (RABBIT) Antibody DyLight 549 Conjugated - 600-442-384 Rockland Cat# 600-442-384
anti-HA
DOI: 10.3390/cancers12071989
Resource: (Abcam Cat# ab18181, RRID:AB_444303)
Curator: @Naa003
SciCrunch record: RRID:AB_444303
Curator comments: HA tag antibody [HA.C5] Abcam Cat# ab18181
anti‐Myc
DOI: 10.1111/bph.15023
Resource: (Cell Signaling Technology Cat# 2276, RRID:AB_331783)
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SciCrunch record: RRID:AB_331783
Curator comments: Mouse Anti-Myc-Tag Monoclonal Antibody, Unconjugated, Clone 9B11 Cell Signaling Technology Cat# 2276
HA-Tag (6E2) mouse mAb (Alexa Fluor 488 conjugate)
DOI: 10.1016/j.chembiol.2020.03.004
Resource: (Cell Signaling Technology Cat# 2350, RRID:AB_491023)
Curator: @ethanbadger
SciCrunch record: RRID:AB_491023
2367s
DOI: 10.1101/gad.332395.119
Resource: (Cell Signaling Technology Cat# 2367, RRID:AB_10691311)
Curator: @Naa003
SciCrunch record: RRID:AB_10691311
Curator comments: HA-Tag (6E2) Mouse mAb antibody Cell Signaling Technology Cat# 2367
HA
DOI: 10.1101/gad.332395.119
Resource: (Cell Signaling Technology Cat# 3724, RRID:AB_1549585)
Curator: @Naa003
SciCrunch record: RRID:AB_1549585
Curator comments: Rabbit Anti-HA-Tag Monoclonal Antibody, Unconjugated, Clone C29F4 Cell Signaling Technology Cat# 3724
HA
DOI: 10.2337/db19-0508
Resource: (Cell Signaling Technology Cat# 3724, RRID:AB_1549585)
Curator: @Naa003
SciCrunch record: RRID:AB_1549585
Curator comments: Rabbit Anti-HA-Tag Monoclonal Antibody, Unconjugated, Clone C29F4 Cell Signaling Technology Cat# 3724
FLAG-tag
DOI: 10.2337/db19-0508
Resource: (Sigma-Aldrich Cat# F1804, RRID:AB_262044)
Curator: @Naa003
SciCrunch record: RRID:AB_262044
Curator comments: Monoclonal ANTI-FLAG® M2 antibody Sigma-Aldrich Cat# F1804
MYC-ta
DOI: 10.2337/db19-0508
Resource: (Millipore Cat# 05-724, RRID:AB_309938)
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SciCrunch record: RRID:AB_309938
Curator comments: Anti-Myc Tag, clone 4A6 antibody Millipore Cat# 05-724
anti-HA tag
DOI: 10.3233/CBM-190993
Resource: (Abcam Cat# ab130275, RRID:AB_11156884)
Curator: @Naa003
SciCrunch record: RRID:AB_11156884
Curator comments: HA tag antibody [16B12] Abcam Cat# ab130275
anti-6 ××<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" alttext="\times" display="inline" id="S2.SS8.p2.m3"><mml:mo>×</mml:mo></mml:math> His tag
DOI: 10.3233/CBM-190993
Resource: (Abcam Cat# ab18184, RRID:AB_444306)
Curator: @Naa003
SciCrunch record: RRID:AB_444306
Curator comments: 6X His tag® antibody [HIS.H8] Abcam Cat# ab18184
Mouse anti Histidine Tag
DOI: 10.1016/j.cell.2020.04.031
Resource: (Bio-Rad Cat# MCA1396, RRID:AB_322084)
Curator: @ethanbadger
SciCrunch record: RRID:AB_322084
HA-tag
DOI: 10.3390/ijms21051773
Resource: (Cell Signaling Technology Cat# 3724, RRID:AB_1549585)
Curator: @Naa003
SciCrunch record: RRID:AB_1549585
Curator comments: Rabbit Anti-HA-Tag Monoclonal Antibody, Unconjugated, Clone C29F4 Cell Signaling Technology Cat# 3724
anti-V5 antibody
DOI: 10.1038/s41586-020-1947-z
Resource: (Thermo Fisher Scientific Cat# R960-25, RRID:AB_2556564)
Curator: @evieth
SciCrunch record: RRID:AB_2556564
Curator comments: Thermo Fisher Scientific Cat# R960-25, V5 Tag Monoclonal Antibody
Note: This rebuttal was posted by the corresponding author to Review Commons. Content has not been altered except for formatting.
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Reviewer 1
__*Review 1 Summary:
__In this manuscript, Borah et al showed that Heh2, a component of INM, can be co-purified with a specific subset of nucleoporins. They also found that disrupting interactions between Heh2 and NPC causes NPC clustering. Lastly, they showed that the knockout of Nup133, which does not physically interact with Heh2, causes the dissociation of Heh2 from NPCs. These findings led the authors to propose that Heh2 acts as a sensor of NPC assembly state. *
__Reviewer 1 major comment 1:__ The authors claimed that Heh2 acts as a sensor of NPC assembly state, as evidenced by their finding that Heh2 fails to bind with NPCs in nup133 Δ cells (Fig2, Fig 5). However, there is a possibility that the association between Heh2 and NPCs is merely affected by the clustering of the NPCs (as the authors discussed) but not related to the structural integrity of NPC.
Our Response: We agree that this is a possibility, however, we ask the reviewer to also consider that we artificially cluster NPCs using the anchor away system (Figure 3C) and this does not affect Heh2’s association with NPCs. Thus, clustering per se is insufficient to disrupt Heh2 binding to NPCs. We will also make changes in the text to make this point.
Reviewer 1 major comment 2: In addition, their data showing that the Heh2-NPCs association is not easily disrupted by knocking out the individual components of the IRC (Fig. 5A and 5D), also disfavor the idea that Heh2 could sense NPC assembly state.
Our Response: There are three considerations here. The first is that as this is the first evidence of any kind of “NPC assembly state” sensor, it is difficult to make any assumptions as to what specifically such a sensor would be monitoring. i.e. perhaps sensing only the ORC is what is functionally important. Second, for obvious reasons, we only tested non-essential IRC nups so by definition there is inherent functional redundancy that maintains NPC function and thus there may be no need to “sense” anything in the absence of these IRC nups. Further (and last), the IRC is essential for NPC assembly. Thus, without an IRC there is no NPC assembly state to sense.
Reviewer 1 major comment 3: Since some nup knockout strains, other than nup133 Δ, are also known to show the NPC clustering (ex. nup159 (Gorsch JCB 1995) and nup120 (Aitchison JCB 1995; Heath JCB 1995)), it will be worth trying to monitor the localization of Heh2 and its interaction with nucleoporins (by Heh2-TAP) using these strains. While Nup159 is a member of the cytoplasmic complex, Nup120 is an ORC nucleoporin. Thus, biochemical and phenotypical analysis using these mutant cells will be useful to clarify if the striking phenotypes the authors found are specific to nup133 knockout strain (or ORC Nup knockouts) or could be commonly observed in the strains that show NPC clustering. Another interesting point is that Nup159 shows strong interaction with Heh2, even in nup133Δ cells. As the authors mentioned, Nup159-Heh2 interaction may not be sufficient for Heh2-NPC association, but it could be important for NPC clustering.
Our Response: These are excellent points and we agree that there is a need to more thoroughly explore how NPC clustering driven by abrogating the function of other nups impacts Heh2’s association with NPCs. Thus, in a revised manuscript, we would examine Heh2’s association with NPCs in several additional genetic backgrounds where NPCs cluster.
Reviewer 1 major comment 4: Figure 4C: Is it known that rapamycin treatment in this strain did not affect the protein levels of nucleoporins? Otherwise, the authors should confirm this by western blotting (at least some of them).
Our Response: This is a good point and we will directly address this with Western blotting of some nups.
Reviewer 1 major comment 5: Figure 5: The authors mentioned (line 256-257) that "in all cases the punctate, NPC-like distribution of Heh2-GFP was retained (Fig 5D)". However, nup107 KO strain seems to show more diminished punctate staining as compared with other strains. To clarify this, the authors should express mCherry tagged Nup as in Fig. 2 or Fig. 3.
Our Response: Yes, we agree and in fact this observation is consistent with the fact that there is an ER-pool of Heh2 observed in this strain and we observe loss of nup interactions in the affinity purification. We will include a more thorough quantification of this in a revised manuscript and more directly address this in the text.
**Minor comments:**
Reviewer 1 minor comment 1: Figure 4A and 4B: The authors should show Scatter plot as in Fig. 2 and Fig. 3.
We will include this in a revised manuscript.
Reviewer 1 minor comment 2: Figure 5C: Explanations of the arrowheads is missing in the figure legend.
Thank you for pointing this out, it will be fixed in a revised manuscript.
Reviewer 1 minor comment 3: Figure 6: Is there any information as to where Heh2 (316-663) is localized in the cell?
As this truncation lacks INM targeting sequences, it is found throughout the cortical ER. The determinants of Heh2 targeting (including truncations) has been extensively evaluated in King et al. 2006, Meinema et al., 2011 and Rempel et al. 2020. We will make this clearer in the revised manuscript.
Reviewer 1 minor comment 4: Figure 6B: Nucleoporins should be marked with color circles as in Fig. 1 and Fig. 5.
This will be done.
Reviewer 2
Borah et al. present a biochemical and cell biological examination of the inner nuclear membrane (INM) protein Heh2 and its putative interactions with the nuclear pore complex (NPC). The potential conceptual advance of this study is that Heh2 interacts with the NPC, while mutations believed to trigger NPC mis-assembly are shown to abolish interaction with Heh2, leading to the hypothesis that Heh2 is a sensor for NPC assembly states within the (INM). The conclusions would undoubtably be of broad interest to the nucleocytoplasmic transport field, but the evidence provided thus far is insufficient to build confidence and consequently this manuscript is premature for publication.
Our Response: We thank the reviewer for recognizing the potential for a significant conceptual advance for the field but object to the notion that the work is “premature for publication”. This is a highly subjective statement that does not seem to meet the mission or purpose of the Review Commons platform. While it is possible that some of the conclusions drawn in our manuscript might not be fully supported by the data in its current form, there is a substantial body of work here that is certainly publishable.
Reviewer 2 major comment 1: The TAP-tag Heh1/Heh2 pulldowns are the most significant experiment presented, and on face value provide compelling evidence that Heh2 interacts with the NPC. It is stated that mass spectroscopy (MS) was used to confirm the identities of the labeled bands yet there is no methods section, nor any MS data reported in the manuscript. Given the large number of unspecified proteins observed in these gels, and the single-step pulldown methodology used, knowledge of the contaminants present may aid in elucidating how Heh2 pulls down NPC components. Consequently, within the supplementary materials, the authors must indicate which regions of the gel were excised for MS analysis and provide a table listing all of the proteins that were detected for each sample, including the number of unique/expected peptides observed. Our Response: This was a major oversight on our part and a revised manuscript will contain all relevant details with regards to the MS analysis including a more detailed description of the excised bands and the quantification of spectra derived from these bands.
Reviewer 2 major comment 2a: The representative micrographs provided across Figures 2, 3, 4, 5 and 6 are very noisy. Particularly in the case of the mCherry labeled nucleoporins, this is both unusual and unfortunate given this is used to infer colocalization of Heh2 with the NPC.
Our Response: These micrographs are not unusual and are in fact of respectable quality. We agree that the apparent “noise” is unfortunate, but this is simply a reality of the yeast system. We remind the reviewer that there are only ~100 to ~200 NPCs per budding yeast nucleus, which is an order of magnitude smaller than a typical mammalian cell nucleus. Further, the copy number of yeast nups per NPC is half of the mammalian cell NPC. Further, budding yeast are spherical with a cell wall that is extremely effective at scattering light; they are also highly autofluorescent (particularly in the red channel). Lastly, unlike in mammalian cells, budding yeast NPCs are mobile on the nuclear envelope. Thus, co-localization is challenging (particularly with the long exposures required to obtain good images). This is why clustering of NPCs driven by nup133**∆ cells has provided one of the key assays in the field to assess whether a given protein associates with NPCs at the level of light microscopy.
Reviewer 2 major comment 2b: As a result it is unclear whether this experiment can be used to differentiate between NPC colocalization vs. nuclear envelope colocalization.
Our Response: The reviewer is correct. Co-localization between Heh2-GFP and any Nup-mCherry is insufficient to assess NPC association in WT cells. In fact, as we point out in Figure 3B, at best one can expect a correlation of r = 0.48 for two well established nups. Thus, to further support the conclusion that Heh2 associates with NPCs, we established the Nsp1-FRB NPC clustering assay (Figure 3).
Reviewer 2 major comment 2c: The authors should include negative controls for an alternative NE membrane protein that doesn't bind the NPC, which would be expected to exhibit a reduced level of colocalization with NPC proteins when compared to Heh2. For example, Heh1 would be a suitable, given the clear-cut negative pulldown data and its prior usage as a negative control in Figure 4.
Our Response: This is included in Figure 3D.
Reviewer 2 major comment 3a. Figure 2. The rim staining for the Nup82-mCherry in the WT background is unusually punctate, bringing into question the viability of the cells imaged.
Our Response: As the middle cell in the panel is undergoing cell division, these cells are clearly viable. All our imaging is performed on mid-log phase cultures.
Reviewer 2 major comment 3b. Why has ScNup82, a cytoplasmic filament component, been selected for colocalization experiments when Heh2 is proposed to interact with the inner ring complex?
Our Response: The resolution of a conventional light microscope is, at best, 200 nm in x, y. As NPCs are 100 nm in diameter, even two NPCs side-by-side cannot be resolved. The IRC is tens of nm away from the cytoplasmic filaments thus any nup is relevant for a co-localization analysis with a light microscope.
Reviewer 2 major comment 3c: Additionally, the experiments shown in panels A and C are not directly comparable, ScNup82 is an asymmetric cytoplasmic nucleoporin, while SpNup107 is located in the Y-shaped Nup84 nucleoporin complex and present on both faces of the NPC. This experiment should be repeated with scNup84 to match panel C, additionally a viability dot spot assay and western blot analysis of the labeled proteins should be conducted.
Our response: These are in fact directly comparable within the limits of resolution of light microscopy as described above. Viability assays are not required here as both nups are essential and perturbation to their function would lead to inviability.
Reviewer 2 major comment 4: Figure 3, the authors use yeast strains where proteins are tagged with FRB and FKBP12 domains, which dimerize upon the addition of rapamycin inducing NPC clusters. The authors then observe the effect this has on Heh2 NPC colocalization. However, Rapamycin may also have an effect independent from the induced dimerization event. Negative controls should be performed in strains lacking the FRB and FKBP12 tagged proteins to demonstrate that Rapamycin doesn't modify Heh2 localization independently of NPC clustering.
Our response: This is a good point and important control that we performed in prior studies, see Colombi et al., JCB, 2013. We will be more explicit in describing that this control has been done.
Reviewer 2 major comment 5: Figure 4. The authors provide a qualitative description of the colocalization presented, while in all other instances they calculate a Pearson correlation coefficient. This is significant because Heh2 appears to be evenly distributed within the NE of the DMSO control (panel B). Given the presented hypothesis isn't colocalization expected with Nup192? As a minimum, a Pearson correlation coefficient analysis should be conducted and added to Figure 4.
Our response: This will be included in a revised manuscript.
Reviewer 2 major comment 6: Figure 4. Pom152-mCherry localizes at both the NE and strongly within the cytoplasm, which is unexpected given typical rim staining phenotypes observed previously for both Pom152-YFP and Pom152-GFP strains (Katta, ..., Jaspersen et al., Genetics (2015) & Upla, ..., Fernandez-Martinez et al., Structure (2017), respectively). Given the unusually weak rim staining observed throughout, viability assays of the strains listed in Table S1 and protein expression analysis of the tagged nucleoporins via western blot is necessary.
Our response: This is not localization in the cytoplasm but is in fact autofluorescence from the yeast vacuole. We regret we were not more explicit in describing this and we will make the manuscript more accessible for the non yeast expert. In order to perform the Western blot analysis for all strains requested by the reviewer would require a battery of antibodies to the endogenous proteins to directly assess how tagging influences nup levels, which we do not have (nor does anyone else that we are aware of). This is also not standard practice in the field as it is an onerous and unnecessary burden.
Reviewer 2 major comment 7:* Figure 5A. The TAP-tagged pulldowns from ∆Pom152 and ∆Nup133 strains appear to be from a different round of experiments than the previous deletion strains presented. Interestingly, there appears to be an additional band at approximately 250 kDa in both cases that is not present in any other experiments. This band could be a contaminant observed due to different experimental conditions, or a protein that exclusively binds to Heh2 in the ∆Pom152 and ∆Nup133 background. Either way the authors should identify this protein with MS to address this ambiguity.
*
Our response: We will include negative controls for these specific experiments to show that this is a non specific band.
Reviewer 2 major comment 8: Figure 6B. Please label the nucleoporin bands in the TAP-tagged pulldowns.
Our response: This will be done.
Reviewer 2 major comment 9: Figure 6D. Please specify Heh2-GFP clustering in the y-axis.
Our response: As this represents both Heh2-GFP and heh2-1-570-GFP, we will keep it as is to avoid confusion.
Reviewer 2 major comment 10: *Under the results section titled 'Heh2 binds to specific nups in evolutionarily distant yeasts', the authors state that spHeh2 co-purifies with "several specific species". The meaning is unclear, this sentence should be rephrased and the specific species clearly described. **
*
Our response: Ok.
Reviewer 2 major comment 11: Under the results section titled 'Heh2 fails to interact with NPCs lacking Nup133', the authors refer to a Pearson correlation coefficient of -0.03 as a clear anticorrelation. Instead state there was no correlation.
Our response: Ok.
Reviewer 2 major comment 12: In the discussion, the authors state that "clustering itself may sterically preclude an interaction with Heh2". The text should be expanded to explain this in more detail, it is not clear from the presented data why this would occur.
Our response: Ok.
Reviewer 2 comment on significance: the manuscript is premature for publication.
Our Response: Such a statement has no relevance to this form of review as a decision as to whether a study is premature for publication should be made by journal editors, not reviewers. We would argue quite strongly that we have definitively shown that Heh2 binds to NPCs, that it does so in multiple evolutionarily distant yeasts and that this binding is functionally relevant. For example, we can specifically disrupt the association of Heh2 with NPCs with a specific domain deletion and observe a loss of function phenotype (e.g. NPC clustering). What all three reviewers agree on is that the concept of a “NPC assembly state sensor” needs additional data to be fully supported, although we note that this reviewer did not provide any suggestions for how we might achieve this goal. We further note that we added the qualifier “may” into the title of the work. Thus, we will therefore perform additional experiments as outlined in comments to Reviewer 1 to support this conclusion in order to introduce this as a new concept in the field.
Reviewer Comment from Cross Commenting: It seems to me that all reviewers agree that the manuscript is premature for publication. The data thus far do not support the conclusion that Heh2 may be an NPC assembly sensor nor does it provide any mechanistic insight. Reading the comments of the other two reviewers makes me more negative, as it is care that the paper also lacks scientific rigor. The manuscript is a great starting point for a rigorous dissection but I do not see this paper to be a candidate for a broad impact journal.
Our Response: The statement that this manuscript is premature for publication is an opinion and does not seem to reflect the sentiment of the other reviewers. It is also confounding that this reviewer suggests that this work lacks rigor. With the exception of the omission of the MS analysis (our fault), the data are of high quality and rigorously quantified. Our assertion of rigor and data quality is based on our collective team’s many decades-long history of publishing and reviewing papers at the highest levels in this field. Questions as to the quality of the data as stated by this reviewer (and only this reviewer) in fact address limitations of light microscopy and the yeast system more generally in this one respect.
Reviewer 3
Reviewer 3 Summary part a*: This is quite an interesting manuscript that explores the relationship between an INM protein, Heh2, and NPCs. It represents an extension of earlier work performed by this group in which it was shown that the HEH2 gene shares genetic interactions with the genes encoding various nucleoporins. Heh2 belongs to an intriguing family of conserved proteins that includes its orthologue, Heh1, as well as human MAN1 (LEMD3) and LEMD2, among others. Each of these proteins contains two transmembrane domains with the N- and C-terminal regions extending in to the nucleoplasm. The two TM domains are separated by a short lumenal loop.
In this study, the authors show that a population of Heh2 is associated with Nups of the NPC inner ring complex. This was demonstrated initially in pulldown experiments. The authors go on to show that when NPCs are caused to aggregate, by physical tethering employing an FKBP/FRP system in combination with Rapamycin, Heh2, but not Heh1, colocalizes with the NPC clusters. *
Our Response: Thank you to the reviewer for recognizing the value of this work.
Reviewer 3 Summary_b. Although not stated explicitly in the manuscript, this would imply that there is a population of Heh2 that resides in the NPC membrane domain, with the remainder in the INM. As an idle question, is there any evidence for a similar localization of MAN1 or LEMD2 in mammals? I am guessing probably not.
Our Response: We regret this was not made more clear but the idea that there is a pool of Heh2 at the POM and a pool at the INM is an important conclusion of the work and was stated in the results - we’ll re-emphasize in the revised discussion. As to whether MAN1 or LEMD2 has a similar NPC association, we hypothesize that MAN1 but not LEMD2 will indeed interact with NPCs in mammalian cells. This is based on considering that we show that both the budding and fission yeast orthologues of MAN1 share this association so unless it was lost in evolution, this is a likely outcome of future studies.
Reviewer 3 Significance statement a: The complications arise when the authors show that an alternative method of NPC aggregation (although they did this first), involving Nup133 deletion, results in failure of Heh2 to co-aggregate. In other words, Nup133 is required for the association of Heh2 with NPCs. The issue here is that there is no evidence for an interaction between Heh2 and Nup133, and furthermore that loss of Nup133 (a Y complex component of the outer ring complex) leaves the inner ring complex intact.
Our Response: We tested the nup133Δ background first as this is the standard approach for assessing NPC-association of a given protein so we felt this would be logical for a reader in the field. Further, while the disruption of Heh2’s binding by loss of Nup133 may be a complication, we prefer to see it as an opportunity for discovery. As described in our manuscript, we have chosen to interpret this result in the context of a new biological function/concept with Heh2 being a novel “NPC assembly state” sensor. While one could argue that we have not fully met this bar yet, we will perform additional experiments as outlined in our response to reviewer 1 to help support this compelling conclusion.
Reviewer 3 Signfiicance statement b: What is clear, however, is that Heh2 seems to be required to inhibit NPC aggregation since Heh2 deficient cells exhibit NPC clusters. The association between Heh2 and IRC Nups resides in the C-terminal nucleoplasmic winged helix domain. The N-terminal domain, in contrast confers INM localization.
Our Response: We agree.__*
Reviewer 3 Signfiicance statement c I must admit, I am in two minds about this manuscript. The data clearly show that Heh2 is associated with IRC components and I agree with the authors that this protein may well have a role in NPC assembly quality control perhaps in the guise of a chaperone. However, I find it hard to come up with a convincing model for the effects of Nup133. On the one hand, one could make an argument that the data presented here is too preliminary and fails to provide a complete story. On the other hand, it does provide an intriguing foundation for future studies and I do feel positively disposed towards it. In short, I have no fundamental complaints about the science, I am just uncertain as to whether the study is ready for publication.
Our Response: This statement nicely articulates the challenge with this manuscript as there are some solid findings (that Heh2 binds specifically to NPCs etc.) but also a provocative finding (that loss of Nup133 breaks Heh2’s interaction with NPCs despite not physically interacting). Thus, there is a decision to be made about whether there is value in introducing a novel concept to the field once additional data is provided in a revised manuscript.
Reviewer 3 Cross commenting: I have no fundamental disagreements with either of the other two reviewers. The comment from Reviewer#2 summarises this quite neatly. While I have fewer concerns about the quality of the data as presented, I think we all agree that at best the study is preliminary. What the authors need to do is to construct a coherent model that will account for the observations described here and then to design experiments that will test this model. I'm not suggesting that they must have a complete story, but they do need to go beyond what is in the current manuscript.
Our Response: We appreciate that the reviewer does not have any questions about the quality of our data, but we argue that we have in fact presented the most coherent interpretation of the data as it currently stands. As described above, we intend to attempt to solidify this model by performing experiments suggested by reviewer 1.
Note: This preprint has been reviewed by subject experts for Review Commons. Content has not been altered except for formatting. Reply to the Reviewers I thank the Referees for their...Referee #1__
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