Activation of Myosin-I by Members of the Ste20p Protein Kinase Family

Autor: Cunle Wu, David Y. Thomas, Emilia Furmaniak-Kazmierczak, Ekkehard Leberer, Sheu-Fen Lee, Graham P. Côté
Rok vydání: 1996
Předmět:
Zdroj: Journal of Biological Chemistry. 271:31787-31790
ISSN: 0021-9258
DOI: 10.1074/jbc.271.50.31787
Popis: The heavy chain of myosin-ID isolated from Dictyostelium was identified as an in vitro substrate for members of the Ste20p family of serine/threonine protein kinases which are thought to regulate conserved mitogen-activated protein kinase pathways. Yeast Ste20p and Cla4p and mammalian p21-activated protein kinase (PAK) phosphorylated the heavy chain to 0.5-0.6 mol of Pi/mol and stimulated the actin-dependent Mg2+-ATPase activity to an extent equivalent to that of the Ste20p-like myosin-I heavy chain kinase isolated from Dictyostelium. PAK purified from rat brain required GTPgammaS-Cdc42 to express full activity, whereas recombinant mouse mPAK3 fused to glutathione S-transferase and purified from bacteria, and Ste20p and Cla4p purified from yeast extracts were fully active without GTPgammaS-Cdc42. These results suggest, together with the high degree of structural and functional conservation of Ste20p family members and myosin-I isoforms, that myosin-I activation by Ste20p family protein kinases may contribute to the regulation of morphogenetic processes in organisms ranging from yeast to mammalian cells.
Databáze: OpenAIRE