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.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 27, 2002, 5:40 a.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 10:35 p.m.) |
Indexed | 1 month, 1 week ago (July 23, 2025, 9:03 a.m.) |
Issued | 26 years, 5 months ago (March 26, 1999) |
Published | 26 years, 5 months ago (March 26, 1999) |
Published Print | 26 years, 5 months ago (March 26, 1999) |
@article{Sanders_1999, title={Inhibition of Myosin Light Chain Kinase by p21-Activated Kinase}, volume={283}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.283.5410.2083}, DOI={10.1126/science.283.5410.2083}, number={5410}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Sanders, Luraynne C. and Matsumura, Fumio and Bokoch, Gary M. and de Lanerolle, Primal}, year={1999}, month=mar, pages={2083–2085} }