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Article

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

FEBS letters - 2 Jun 2000

Pelpel K, Leibovitch M, Fernandez A, Leibovitch S A

Abstract excerpt

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...

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Source

Identifiers

PMID: 10838091
DOI: 10.1016/s0014-5793(00)01610-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Research trail→

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Mutation of MyoD-Ser237 abolishes its up-regulation by c-Mos.PMID 10838091Read ↗

Mos activates myogenic differentiation by promoting heterodimerization of MyoD and E12 proteins.Semantic proximity Read ↗

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Monoclonal antibodies identify a possible regulatory domain of MyoD1.Semantic proximity Read ↗

Casein kinase II increases the transcriptional activities of MRF4 and MyoD independently of their direct phosphorylation.Semantic proximity Read ↗

Evidence that E-box promoter elements and MyoD transcription factors play a role in the induction of cathepsin B gene expression during human myoblast differentiation.Semantic proximity Read ↗

Inhibition of v-Mos kinase activity by protein kinase A.Semantic proximity Read ↗

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