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

被引：121

作者：

Murata-Hori, M ^{[1
]}

Suizu, F ^{[1
]}

Iwasaki, T ^{[1
]}

Kikuchi, A ^{[1
]}

Hosoya, H ^{[1
]}

机构：

[1] Hiroshima Univ, Fac Sci, Dept Biol Sci, Higashihiroshima 7398526, Japan

来源：

FEBS LETTERS | 1999年 / 451卷 / 01期

关键词：

regulatory light chain of myosin II; zipper-interacting protein kinase; phosphorylation; myosin light chain kinase; actin-activated MgATPase activity; cytokinesis;

D O I：

10.1016/S0014-5793(99)00550-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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, (C) 1999 Federation of European Biochemical Societies.

引用

页码：81 / 84

页数：4

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