Report

Inhibition of Myosin Light Chain Kinase by p21-Activated Kinase

+ See all authors and affiliations

Science  26 Mar 1999:
Vol. 283, Issue 5410, pp. 2083-2085
DOI: 10.1126/science.283.5410.2083

You are currently viewing the abstract.

View Full Text

Abstract

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.

  • * To whom correspondence should be addressed. E-mail: bokoch{at}scripps.edu; primal{at}uic.edu

View Full Text

Related Content