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Updated: Aug 16, 2026

Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry
Published on: May 17, 2016
Mutation of MyoD-Ser237 abolishes its up-regulation by c-Mos
K Pelpel1, M Leibovitch, A Fernandez
1Laboratoire de Génétique Oncologique, UMR 1599, CNRS Institut Gustave Roussy, Villejuif, France.
Abstract:
Recently we have shown that Mos could activate myogenic differentiation by promoting heterodimerisation of MyoD and E12 proteins. Here, we demonstrate that MyoD can be efficiently phosphorylated by in vitro kinase assay with purified Mos immunoprecipitated from transfected cells. Comparative two-dimensional tryptic phosphopeptide mapping combined with site-directed mutagenesis revealed that Mos phosphorylates MyoD on serine 237. Mutation of serine 237 to a non-phosphorylable alanine (MyoD-Ala237) abolished the positive regulation of MyoD by Mos following overexpression in proliferating 10T1/2 cells. Taken together, our data show that direct phosphorylation of MyoD-Ser237 by Mos plays a positive role in increasing MyoD activity during myoblast proliferation.
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