Evidence map›Paper›PMID 9658178›Full record

ArticleMolecular biology of the cell1998

RhoA GTPase and serum response factor control selectively the expression of MyoD without affecting Myf5 in mouse myoblasts.

G Carnac, M Primig, M Kitzmann, P Chafey, D Tuil, N Lamb, A Fernandez

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

54 citing papers in PubMed, 122 citations in OpenAlex.

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  9. The STARS signaling pathway: a key regulator of skeletal muscle function.Pflugers Archiv : European journal of physiology · 2014
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  17. N-cadherin ligation, but not Sonic hedgehog binding, initiates Cdo-dependent p38alpha/beta MAPK signaling in skeletal myoblasts.Proceedings of the National Academy of Sciences of the United States of America · 2010
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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

7 authors at 3 institutions in 1 country.

G CarnacCell Biology Unit, IGH, Centre National de la Recherche Scientifique, UPR 1142, 34396 Montpellier cédex 5, France.
M Primig
M Kitzmann
P Chafey
D Tuil
N Lamb
A Fernandez
Centre National de la Recherche Scientifique · FRInserm · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MyoD and Myf5 belong to the family of basic helix-loop-helix transcription factors that are key operators in skeletal muscle differentiation. MyoD and Myf5 genes are selectively activated during development in a time and region-specific manner and in response to different stimuli. However, molecules that specifically regulate the expression of these two genes and the pathways involved remain to be determined. We have recently shown that the serum response factor (SRF), a transcription factor involved in activation of both mitogenic response and muscle differentiation, is required for MyoD gene expression. We have investigated here whether SRF is also involved in the control of Myf5 gene expression, and the potential role of upstream regulators of SRF activity, the Rho family G-proteins including Rho, Rac, and CDC42, in the regulation of MyoD and Myf5. We show that inactivation of SRF does not alter Myf5 gene expression, whereas it causes a rapid extinction of MyoD gene expression. Furthermore, we show that RhoA, but not Rac or CDC42, is also required for the expression of MyoD. Indeed, blocking the activity of G-proteins using the general inhibitor lovastatin, or more specific antagonists of Rho proteins such as C3-transferase or dominant negative RhoA protein, resulted in a dramatic decrease of MyoD protein levels and promoter activity without any effects on Myf5 expression. We further show that RhoA-dependent transcriptional activation required functional SRF in C2 muscle cells. These data illustrate that MyoD and Myf5 are regulated by different upstream activation pathways in which MyoD expression is specifically modulated by a RhoA/SRF signaling cascade. In addition, our results establish the first link between RhoA protein activity and the expression of a key muscle regulator.

Indexed as

Botulinum Toxins3T3 CellsADP Ribose TransferasesAnimalsCell LineDNA-Binding ProteinsGene Expression RegulationGenes, DominantGTP-Binding ProteinsGTP PhosphohydrolasesMiceMuscle ProteinsMuscle, SkeletalMyoD ProteinMyogenic Regulatory Factor 5Nuclear ProteinsADP Ribose TransferasesBotulinum ToxinsDNA-Binding Proteinsexoenzyme C3, Clostridium botulinumGTP-Binding ProteinsGTP PhosphohydrolasesMuscle ProteinsMyf5 protein, mouseMyoD ProteinMyogenic Regulatory Factor 5Nuclear ProteinsRepressor ProteinsrhoA GTP-Binding ProteinSerum Response FactorTrans-Activators

Identifiers

PMID9658178
PMCPMC25431
OpenAlexW2147927258

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.