ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells

FEBS Letters

Kikuchi, Asako¹  Iwasaki, Takahiro¹  Hosoya, Hiroshi¹  Murata-Hori, Maki¹  Suizu, Futoshi¹ 

[1] Department of Biological Science, Faculty of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan

关键词: Regulatory light chain of myosin II;    Zipper-interacting protein kinase;    Phosphorylation;    Myosin light chain kinase;    Actin-activated MgATPase activity;    Cytokinesis;   

DOI  :  10.1016/S0014-5793(99)00550-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel myosin light chain kinase (MLCK) cDNA was isolated from a HeLa cell cDNA library. The deduced amino acid sequence was identical to that of a zipper-interacting protein kinase (ZIPK) which mediates apoptosis [Kawai et al. (1998) Mol. Cell. Biol. 18, 1642–1651]. Here we found that HeLa ZIPK phosphorylated the regulatory light chain of myosin II (MRLC) at both serine 19 and threonine 18 in a Ca²⁺/calmodulin independent manner. Phosphorylation of myosin II by HeLa ZIPK resulted in activation of actin-activated MgATPase activity of myosin II. HeLa ZIPK is the first non-muscle MLCK that phosphorylates MRLC at two sites.

【 授权许可】

Unknown