LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics

doi:10.1083/jcb.200203126

Published 28 May 2002. doi:10.1083/jcb.200203126

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© The Rockefeller University Press, 0021-9525/2002/5/831 $5.00
The Journal of Cell Biology, Volume 157, Number 5, May 28, 2002 831-838

Article

LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics

Olivier Geneste, John W. Copeland and Richard Treisman

Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, London WC2A 3PX, UK

Address correspondence to Richard Treisman, Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, Transcription Laboratory, Room 401, 44 Lincoln's Inn Fields, London WC2A 3PX, UK. Tel.: 44-207-269-3271. Fax: 44-207-269-3093. E-mail: richard.treisman{at}cancer.org.uk

The small GTPase RhoA controls activity of serum response factor(SRF) by inducing changes in actin dynamics. We show that inPC12 cells, activation of SRF after serum stimulation is RhoAdependent, requiring both actin polymerization and the Rho kinase(ROCK)–LIM kinase (LIMK)–cofilin signaling pathway,previously shown to control F-actin turnover. Activation ofSRF by overexpression of wild-type LIMK or ROCK-insensitiveLIMK mutants also requires functional RhoA, indicating thata second RhoA-dependent signal is involved. This is providedby the RhoA effector mDia: dominant interfering mDia1 derivativesinhibit both serum- and LIMK-induced SRF activation and reducethe ability of LIMK to induce F-actin accumulation. These resultsdemonstrate a role for LIMK in SRF activation, and functionalcooperation between RhoA-controlled LIMK and mDia effector pathways.

Key Words: LIM kinase; mDia; ROCK; actin; SRF

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