Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization

Neng Yang, Osamu Higuchi, Kazumasa Ohashi, Kyoko Nagata, Atsushi Wada, Kenji Kangawa, Eisuke Nishida and Kensaku Mizuno ()
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Neng Yang: Faculty of Science, Kyushu University
Osamu Higuchi: Faculty of Science, Kyushu University
Kazumasa Ohashi: Faculty of Science, Kyushu University
Kyoko Nagata: Faculty of Science, Kyushu University
Atsushi Wada: Graduate School of Science, Kyoto University
Kenji Kangawa: National Cardiovascular Center Research Institute
Eisuke Nishida: Graduate School of Science, Kyoto University
Kensaku Mizuno: Faculty of Science, Kyushu University

Nature, 1998, vol. 393, issue 6687, 809-812

Abstract: Abstract Rac is a small GTPase of the Rho family that mediates stimulus-induced actin cytoskeletal reorganization to generate lamellipodia1,2,3,4,5. Little is known about the signalling pathways that link Rac activation to changes in actin filament dynamics. Cofilin is known to be a potent regulator of actin filament dynamics6,7,8,9,10, and its ability to bind and depolymerize actin is abolished by phosphorylation of serine residue at 3 (refs 11, 12); however, the kinases responsible for this phosphorylation have not been identified. Here we show that LIM-kinase 1 (LIMK-1), a serine/threonine kinase containing LIM and PDZ domains13,14,15,16, phosphorylates cofilin at Ser 3, both in vitro and in vivo. When expressed in cultured cells, LIMK-1 induces actin reorganization and reverses cofilin-induced actin depolymerization. Expression of an inactive form of LIMK-1 suppresses lamellipodium formation induced by Rac or insulin. Furthermore, insulin and an active form of Rac increase the activity of LIMK-1. Taken together, our results indicate that LIMK-1 participates in Rac-mediated actin cytoskeletal reorganization, probably by phosphorylating cofilin.

Date: 1998
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DOI: 10.1038/31735

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