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

Nature cell biology | Sep 6, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10559936

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.

Pubmed ID: 10559936 RIS Download

Mesh terms: Actins | Animals | COS Cells | Cell Line | Cell Membrane | Cytoskeleton | Enzyme Activation | Humans | Kinetics | Lim Kinases | Mutagenesis, Site-Directed | Phosphorylation | Phosphothreonine | Protein Kinases | Protein-Serine-Threonine Kinases | Recombinant Proteins | Sequence Deletion | Signal Transduction | Transfection | Zinc Fingers | cdc42 GTP-Binding Protein | p21-Activated Kinases | rac GTP-Binding Proteins

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