Evidence map›Paper›PMID 28275944›Full record

ArticleCell stress & chaperones2017

Fine-tuning of actin dynamics by the HSPB8-BAG3 chaperone complex facilitates cytokinesis and contributes to its impact on cell division.

Alice Anaïs Varlet, Margit Fuchs, Carole Luthold, Herman Lambert, Jacques Landry, Josée N Lavoie

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 39 citations in OpenAlex.

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  15. Viruses go modular.The Journal of biological chemistry · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Alice Anaïs VarletCentre de recherche sur le cancer de l'Université Laval, Québec, Canada.
Margit FuchsCentre de recherche sur le cancer de l'Université Laval, Québec, Canada.
Carole LutholdCentre de recherche sur le cancer de l'Université Laval, Québec, Canada.
Herman LambertCentre de recherche sur le cancer de l'Université Laval, Québec, Canada.
Jacques LandryCentre de recherche sur le cancer de l'Université Laval, Québec, Canada.
Josée N LavoieCentre de recherche sur le cancer de l'Université Laval, Québec, Canada. josee.lavoie@crchudequebec.ulaval.ca.
Centre hospitalier de l'Université Laval · CAUniversité Laval · CA

Funding

CIHR 7088
6 · The paper itself

Abstract

The small heat shock protein HSPB8 and its co-chaperone BAG3 are proposed to regulate cytoskeletal proteostasis in response to mechanical signaling in muscle cells. Here, we show that in dividing cells, the HSPB8-BAG3 complex is instrumental to the accurate disassembly of the actin-based contractile ring during cytokinesis, a process required to allow abscission of daughter cells. Silencing of HSPB8 markedly decreased the mitotic levels of BAG3 in HeLa cells, supporting its crucial role in BAG3 mitotic functions. Cells depleted of HSPB8 were delayed in cytokinesis, remained connected via a disorganized intercellular bridge, and exhibited increased incidence of nuclear abnormalities that result from failed cytokinesis (i.e., bi- and multi-nucleation). Such phenotypes were associated with abnormal accumulation of F-actin at the intercellular bridge of daughter cells at telophase. Remarkably, the actin sequestering drug latrunculin A, like the inhibitor of branched actin polymerization CK666, normalized F-actin during cytokinesis and restored proper cell division in HSPB8-depleted cells, implicating deregulated actin dynamics as a cause of abscission failure. Moreover, this HSPB8-dependent phenotype could be corrected by rapamycin, an autophagy-promoting drug, whereas it was mimicked by drugs impairing lysosomal function. Together, the results further support a role for the HSPB8-BAG3 chaperone complex in quality control of actin-based structure dynamics that are put under high tension, notably during cell cytokinesis. They expand a so-far under-appreciated connection between selective autophagy and cellular morphodynamics that guide cell division.

Indexed as

CytokinesisActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCell DivisionGene Knockdown TechniquesHeat-Shock ProteinsHeLa CellsHumansMolecular ChaperonesProtein Serine-Threonine KinasesActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBAG3 protein, humanHeat-Shock ProteinsHSPB8 protein, humanMolecular ChaperonesProtein Serine-Threonine KinasesActinAutophagyBAG3CytokinesisHSPB8

Identifiers

PMID28275944
PMCPMC5465032
OpenAlexW2593876335

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.