Phosphorylation of myogenin at serine 43 by a CDC2-like proline-directed kinase regulates its structural properties and potentially its activity during skeletal muscle differentiation.
Does not support clinical translation; leaves open myogenin’s role in human muscle development.
Myogenin, a member of the MyoD family which governs skeletal muscle differentiation, was identified as a pair of phosphorylated bands on SDS-PAGE during myogenesis. The slow migrating form was found to be hyperphosphorylated myogenin. In vitro phosphorylation by CDC2 kinase caused a prominent reduction in electrophoretic mobility of myogenin. Furthermore, we demonstrated that phosphorylation of the serine residue at position 43 contributes to the modification of myogenin in vivo and in vitro resulting in the reduction in electrophoretic mobility. We propose here that a CDC2-like proline-directed kinase regulates myogenin activity through its phosphorylation.
No takes yet. Share an insight, caveat, or question.
Hashimotoa et al. (1994) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: