Mutation of MyoD‐Ser237 abolishes its up‐regulation by c‐Mos

FEBS Letters

Pelpel, Karine²  Leibovitch, Serge A.²  Fernandez, Anne¹  Leibovitch, Marie-Pierre² 

[1] Institut de Génétique Humaine, UPR 1142, CNRS, 34396 Montpellier Cedex 5, France;Laboratoire de Génétique Oncologique, UMR 1599, CNRS, Institut Gustave Roussy, 39 rue Camille Desmoulins, 94805 Villejuif, France

关键词: c-Mos;    MyoD;    Phosphorylation;    Myogenesis;   

DOI  :  10.1016/S0014-5793(00)01610-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown