Phosphorylation of a proline-directed kinase motif is responsible for structural changes in myogenin.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hashimoto N,Ogashiwa M,Okumura E,Endo T,Iwashita S,Kishimoto T

doi

10.1016/0014-5793(94)00964-3

subject

Has Abstract

pub_date

1994-09-26 00:00:00

pages

236-42

issue

2

eissn

0014-5793

issn

1873-3468

journal_volume

352

pub_type

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