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Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics.

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Affiliations

  • 1. Department of Chemistry, University of California at San Diego, La Jolla 92093-0650, USA.
      Authors
    • Edwards DC 1
    (1 author)

Nature Cell Biology, 01 Sep 1999, 1(5):253-259
https://doi.org/10.1038/12963 PMID: 10559936 

A comment on this article appears in "Close encounters of the LIM-kinase." Nat Cell Biol. 1999 Sep;1(5):E115-7.

Abstract 

Extracellular signals regulate actin dynamics through small GTPases of the Rho/Rac/Cdc42 (p21) family. Here we show that p21-activated kinase (Pak1) phosphorylates LIM-kinase at threonine residue 508 within LIM-kinase's activation loop, and increases LIM-kinase-mediated phosphorylation of the actin-regulatory protein cofilin tenfold in vitro. In vivo, activated Rac or Cdc42 increases association of Pak1 with LIM-kinase; this association requires structural determinants in both the amino-terminal regulatory and the carboxy-terminal catalytic domains of Pak1. A catalytically inactive LIM-kinase interferes with Rac-, Cdc42- and Pak1-dependent cytoskeletal changes. A Pak1-specific inhibitor, corresponding to the Pak1 autoinhibitory domain, blocks LIM-kinase-induced cytoskeletal changes. Activated GTPases can thus regulate actin depolymerization through Pak1 and LIM-kinase.

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