Inhibition of myosin light chain kinase by p21-activated kinase

被引：494

作者：

Sanders, LC

Matsumura, F

Bokoch, GM ^{[1
]}

de Lanerolle, P

机构：

[1] Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA

[3] Rutgers State Univ, Dept Mol Biol & Biochem, Piscataway, NJ 08855 USA

[4] Univ Illinois, Dept Physiol & Biophys, Chicago, IL 60612 USA

来源：

SCIENCE | 1999年 / 283卷 / 5410期

关键词：

D O I：

10.1126/science.283.5410.2083

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

p21-activated kinases (PAKs) are implicated in the cytoskeletal changes induced by the Rho family of guanosine triphosphatases. Cytoskeletal dynamics are primarily modulated by interactions of actin and myosin II that are regulated by myosin light chain kinase (MLCK)-mediated phosphorylation of the regulatory myosin Light chain (MLC). p21-activated kinase 1 (PAK1) phosphorylates MLCK, resulting in decreased MLCK activity. MLCK activity and MLC phosphorylation were decreased, and cell spreading was inhibited in baby hamster kidney-21 and HeLa cells expressing constitutively active PAK1. These data indicate that MLCK is a target for PAKs and that PAKs may regulate cytoskeletal dynamics by decreasing MLCK activity and MLC phosphorylation.

引用

页码：2083 / 2085

页数：3

共 31 条

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