Evidence map›Paper›PMID 25737281›Full record

ArticleGenes & development2015

A KAP1 phosphorylation switch controls MyoD function during skeletal muscle differentiation.

Kulwant Singh, Marco Cassano, Evarist Planet, Soji Sebastian, Suk Min Jang, Gurjeev Sohi, Hervé Faralli, Jinmi Choi, Hong-Duk Youn, F Jeffrey Dilworth and 1 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed, 84 citations in OpenAlex.

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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

11 authors at 6 institutions in 4 countries.

Kulwant SinghSprott Center for Stem Cell Research, Ottawa Hospital Research Institute, Ottawa, Ontario K1H 8L6, Canada;
Marco CassanoSchool of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland;
Evarist PlanetSchool of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland;
Soji SebastianSprott Center for Stem Cell Research, Ottawa Hospital Research Institute, Ottawa, Ontario K1H 8L6, Canada;
Suk Min JangSchool of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland;
Gurjeev SohiSprott Center for Stem Cell Research, Ottawa Hospital Research Institute, Ottawa, Ontario K1H 8L6, Canada;
Hervé FaralliSprott Center for Stem Cell Research, Ottawa Hospital Research Institute, Ottawa, Ontario K1H 8L6, Canada;
Jinmi ChoiDepartment of Biomedical Sciences and Biochemistry and Molecular Biology, Seoul National University College of Medicine, Seoul 110-799, Korea;
Hong-Duk YounDepartment of Biomedical Sciences and Biochemistry and Molecular Biology, Seoul National University College of Medicine, Seoul 110-799, Korea;
F Jeffrey DilworthSprott Center for Stem Cell Research, Ottawa Hospital Research Institute, Ottawa, Ontario K1H 8L6, Canada; Department of Cellular and Molecular Medicine, University of Ottawa, Ontario K1H 8L6, Canada didier.trono@epfl.ch jdilworth@ohri.ca.
Didier TronoSchool of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland; didier.trono@epfl.ch jdilworth@ohri.ca.
École Polytechnique Fédérale de Lausanne · CHOttawa Hospital Research InstituteStem Cell Network · CANew Generation University College · ETSeoul National University · KRUniversity of Ottawa · CA

Funding

CIHR MOP-77778European Research Council 268721
6 · The paper itself

Abstract

The transcriptional activator MyoD serves as a master controller of myogenesis. Often in partnership with Mef2 (myocyte enhancer factor 2), MyoD binds to the promoters of hundreds of muscle genes in proliferating myoblasts yet activates these targets only upon receiving cues that launch differentiation. What regulates this off/on switch of MyoD function has been incompletely understood, although it is known to reflect the action of chromatin modifiers. Here, we identify KAP1 (KRAB [Krüppel-like associated box]-associated protein 1)/TRIM28 (tripartite motif protein 28) as a key regulator of MyoD function. In myoblasts, KAP1 is present with MyoD and Mef2 at many muscle genes, where it acts as a scaffold to recruit not only coactivators such as p300 and LSD1 but also corepressors such as G9a and HDAC1 (histone deacetylase 1), with promoter silencing as the net outcome. Upon differentiation, MSK1-mediated phosphorylation of KAP1 releases the corepressors from the scaffold, unleashing transcriptional activation by MyoD/Mef2 and their positive cofactors. Thus, our results reveal KAP1 as a previously unappreciated interpreter of cell signaling, which modulates the ability of MyoD to drive myogenesis.

Indexed as

Cell DifferentiationAnimalsCell LineGene Expression Regulation, DevelopmentalMEF2 Transcription FactorsMiceMuscle DevelopmentMuscle, SkeletalMyoblastsMyoD ProteinNuclear ProteinsPhosphorylationRepressor ProteinsSignal TransductionTripartite Motif-Containing Protein 28Mef2d protein, mouseMEF2 Transcription FactorsMyoD ProteinNuclear ProteinsRepressor ProteinsTrim28 protein, mouseTripartite Motif-Containing Protein 28epigeneticsG9aKAP1MSK1 phosphorylationMyoDmyogenesis

Identifiers

PMID25737281
PMCPMC4358404
OpenAlexW1990518016

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.