Evidence map›Paper›PMID 9001254›Full record

ArticleMolecular and cellular biology1997

Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C.

V Sartorelli, J Huang, Y Hamamori, L Kedes

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

154 citing papers in PubMed, 365 citations in OpenAlex.

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  20. A long noncoding RNA,Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

94 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 2 countries.

V SartorelliInstitute for Genetic Medicine and Department of Biochemistry and Molecular Biology, University of Southern California School of Medicine, Los Angeles 90033, USA.
J Huang
Y Hamamori
L Kedes
University of Southern California · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By searching for molecules that assist MyoD in converting fibroblasts to muscle cells, we have found that p300 and CBP, two related molecules that act as transcriptional adapters, coactivate the myogenic basic-helix-loop-helix (bHLH) proteins. Coactivation by p300 involves novel physical interactions between p300 and the amino-terminal activation domain of MyoD. In particular, disruption of the FYD domain, a group of three amino acids conserved in the activation domains of other myogenic bHLH proteins, drastically diminishes the transactivation potential of MyoD and abolishes both p300-mediated coactivation and the physical interaction between MyoD and p300. Two domains of p300, at its amino and carboxy terminals, independently function to both mediate coactivation and physically interact with MyoD. A truncated segment of p300, unable to bind MyoD, acts as a dominant negative mutation and abrogates both myogenic conversion and transactivation by MyoD, suggesting that endogenous p300 is a required coactivator for MyoD function. The p300 dominant negative peptide forms multimers with intact p300. p300 and CBP serve as coactivators of another class of transcriptional activators critical for myogenesis, myocyte enhancer factor 2 (MEF2). In fact, transactivation mediated by the MEF2C protein is potentiated by the two coactivators, and this phenomenon is associated with the ability of p300 to interact with the MADS domain of MEF2C. Our results suggest that p300 and CBP may positively influence myogenesis by reinforcing the transcriptional autoregulatory loop established between the myogenic bHLH and the MEF2 factors.

Indexed as

AcetyltransferasesTATA-Binding Protein Associated FactorsTranscription Factor TFIID3T3 CellsActinsAnimalsCell Cycle ProteinsCell DifferentiationCell LineCreatine KinaseCREB-Binding ProteinCyclin-Dependent Kinase Inhibitor p21CyclinsDNA-Binding ProteinsHelix-Loop-Helix MotifsHerpes Simplex Virus Protein Vmw65AcetyltransferasesActinsCDKN1A protein, humanCdkn1a protein, mouseCell Cycle ProteinsCreatine KinaseCREB-Binding ProteinCREBBP protein, humanCrebbp protein, mouseCyclin-Dependent Kinase Inhibitor p21CyclinsDNA-Binding ProteinsHerpes Simplex Virus Protein Vmw65Histone AcetyltransferasesMADS Domain ProteinsMEF2C protein, humanMef2c protein, mouseMEF2 Transcription FactorsMyoD ProteinMyogenic Regulatory FactorsNuclear Proteinsp300-CBP-Associated Factorp300-CBP Transcription FactorsRNA, MessengerTATA-binding protein associated factor 250 kDaTATA-Binding Protein Associated FactorsTrans-ActivatorsTranscription FactorsTranscription Factor TFIID

Identifiers

PMID9001254
PMCPMC231826
OpenAlexW2166021986

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.