Evidence map›Paper›PMID 26933062›Full record

ArticleScience signaling2016

Cytokinesis involves a nontranscriptional function of the Hippo pathway effector YAP.

Duyen Amy Bui, Wendy Lee, Anne E White, J Wade Harper, Ron C J Schackmann, Michael Overholtzer, Laura M Selfors, Joan S Brugge

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 66 citations in OpenAlex.

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  7. Optogenetic control of YAP can enhance the rate of wound healing.Cellular & molecular biology letters · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Duyen Amy BuiDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Wendy LeeThe Ronald O. Perelman Department of Dermatology and the Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA.
Anne E WhiteDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
J Wade HarperDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Ron C J SchackmannDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Michael OverholtzerBCMB (Biochemistry, Cell, and Molecular Biology) Allied Program, Weill Cornell Medical College, 1300 York Avenue, New York, NY 10065, USA. Cell Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Laura M SelforsDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Joan S BruggeDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. joan_brugge@hms.harvard.edu.
Harvard University · USMemorial Sloan Kettering Cancer Center · USNew York University · US

Funding

Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
Network organization and dynamics of the Hippo pathway during oncogenesisF32CA165738 · NCI · HARVARD MEDICAL SCHOOL · PI WHITE, ANNE EILEEN · 2011 to 2014
$156k
NCI NIH HHS 1F32CA165738NCI NIH HHS F32 CA165738NIA NIH HHS AG011085NIA NIH HHS R01 AG011085
6 · The paper itself

Abstract

YAP is a transcriptional coactivator that controls organ expansion and differentiation and is inhibited by the Hippo pathway in cells in interphase. Here, we demonstrated that, during mitosis, YAP localized to the midbody and spindle, subcellular structures that are involved in cytokinesis, the process by which contraction of the cytoskeleton produces two daughter cells. Furthermore, YAP was phosphorylated by CDK1, a kinase that promotes cell cycle progression. Knockdown of YAP by shRNA or expression of a nonphosphorylatable form of YAP delayed the separation of daughter cells (called abscission) and induced a cytokinesis phenotype associated with increased contractile force, membrane blebbing and bulges, and abnormal spindle orientation. Consequently, these defects led to an increased frequency of multinucleation, micronuclei, and aneuploidy. YAP was required for proper localization of proteins that regulate contraction during cytokinesis, including ECT2, MgcRacGap, Anillin, and RHOA. In addition, depletion of YAP increased the phosphorylation of myosin light chain, which would be expected to activate the contractile activity of myosin II, the molecular motor involved in cytokinesis. The polarity scaffold protein PATJ coprecipitated with YAP and colocalized with YAP at the cytokinesis midbody, and knockdown of PATJ phenocopied the cytokinetic defects and spindle orientation alterations induced by either YAP depletion or expression of a nonphosphorylatable YAP mutant. Together, these results reveal an unanticipated role for YAP in the proper organization of the cytokinesis machinery during mitosis through interaction with the polarity protein PATJ.

Indexed as

Adaptor Proteins, Signal TransducingCDC2 Protein KinaseCell LineContractile ProteinsCyclin-Dependent KinasesCytokinesisGTPase-Activating ProteinsHeLa CellsHippo Signaling PathwayHumansImmunoblottingMicroscopy, ConfocalPhosphoproteinsPhosphorylationProtein BindingProtein Serine-Threonine KinasesAdaptor Proteins, Signal TransducinganillinCDC2 Protein KinaseCDK1 protein, humanContractile ProteinsCyclin-Dependent KinasesECT2 protein, humanGTPase-Activating ProteinsmgcRacGAPPATJ protein, humanPhosphoproteinsProtein Serine-Threonine KinasesProto-Oncogene ProteinsrhoA GTP-Binding ProteinTight Junction ProteinsTranscription FactorsYAP1 protein, humanYAP-Signaling Proteins

Identifiers

PMID26933062
PMCPMC5455055
OpenAlexW2289739009

What OpenQuestion holds

Textmetadata
LicenceTDM
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.