Rac‐1 and Raf‐1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase

FEBS Letters

Dunne, Patrick W.¹  Walch, E.Timothy¹  Epstein, Henry F.¹  Wang, Wenfu¹  Shimizu, Miho¹ 

[1] Department of Neurology, NS B302, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA

关键词: Myotonic dystrophy protein kinase;    Rac-1;    Raf-1;    Rho-type GTPases;   

DOI  :  10.1016/S0014-5793(00)01692-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Myotonic dystrophy protein kinase (DMPK) is a serine–threonine protein kinase encoded by the myotonic dystrophy (DM) locus on human chromosome 19q13.3. It is a close relative of other kinases that interact with members of the Rho family of small GTPases. We show here that the actin cytoskeleton-linked GTPase Rac-1 binds to DMPK, and coexpression of Rac-1 and DMPK activates its transphosphorylation activity in a GTP-sensitive manner. DMPK can also bind Raf-1 kinase, the Ras-activated molecule of the MAP kinase pathway. Purified Raf-1 kinase phosphorylates and activates DMPK. The interaction of DMPK with these distinct signals suggests that it may play a role as a nexus for cross-talk between their respective pathways and may partially explain the remarkable pleiotropy of DM.

【 授权许可】

Unknown