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A more recent version of this article appeared on August 17, 2001
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Papers In Press, published online ahead of print June 18, 2001
J. Biol. Chem, 10.1074/jbc.M100871200
Submitted on January 30, 2001
Revised on May 30, 2001
Accepted on June 15, 2001

Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIMK1 and cofilin

Chuntao Dan, April Kelly, Ora Bernard, and Audrey Minden

Biological Sciences, Columbia University, New York, NY 10027

Corresponding Author: agm24{at}columbia.edu

PAK4 is the most recently identified member of the PAK family of serine/threonine kinases. PAK4 differs from other members of the PAK family in sequence and in many of its functions. Previously we have shown that an important function of this kinase is to mediate the induction of filopodia in response to the Rho GTPase Cdc42. Here we show that PAK4 also regulates the activity of the protein kinase LIM Kinase 1 (LIMK1). PAK4 was shown to interact specifically with LIMK1 in binding assays. Immune complex kinase assays revealed that both wild-type and constitutively active PAK4 phosphorylated LIMK1 even more strongly than PAK1, and activated PAK4 stimulated LIMK1?s ability to phosphorylate cofilin. Immunofluorescence experiments revealed that PAK4 and LIMK1 cooperate to induce cytoskeletal changes in C2C12 cells. Furthermore, dominant negative LIMK1 and a mutant cofilin inhibited the specific cytoskeletal and cell shape changes that were induced in response to a recently characterized constitutively activated PAK4 mutant.


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