The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Mutation of MyoD-Ser237 abolishes its up-regulation by c-Mos.

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.[1]


  1. Mutation of MyoD-Ser237 abolishes its up-regulation by c-Mos. Pelpel, K., Leibovitch, M., Fernandez, A., Leibovitch, S.A. FEBS Lett. (2000) [Pubmed]
WikiGenes - Universities