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. 1998 Jun 25;393(6687):809-12.
doi: 10.1038/31735.

Cofilin Phosphorylation by LIM-kinase 1 and Its Role in Rac-mediated Actin Reorganization

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Cofilin Phosphorylation by LIM-kinase 1 and Its Role in Rac-mediated Actin Reorganization

N Yang et al. Nature. .

Abstract

Rac is a small GTPase of the Rho family that mediates stimulus-induced actin cytoskeletal reorganization to generate lamellipodia. 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 dynamics, and its ability to bind and depolymerize actin is abolished by phosphorylation of serine residue at 3; 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 domains, 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.

Comment in

  • Actin, cofilin and cognition.
    Rosenblatt J, Mitchison TJ. Rosenblatt J, et al. Nature. 1998 Jun 25;393(6687):739-40. doi: 10.1038/31597. Nature. 1998. PMID: 9655388 No abstract available.

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