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Papers In Press, published online ahead of print March 13, 2001
Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599-7365
Corresponding Author: Alan_Howe{at}med.unc.edu
The p21-activated kinases (PAKs) are important mediators of cytoskeletal reorganization, cell motility and transcriptional events regulated by the Rho-family GTPases Rac and Cdc42. PAK activation by serum components is strongly dependent on cell adhesion to the extracellular matrix (ECM). PAK binds directly to the Nck adapter protein, an interaction thought to play an important role in regulation and localization of PAK activity. This report demonstrates that the interaction of PAK with Nck is dynamically regulated by cell adhesion. PAK-Nck binding is rapidly lost after cell detachment and rapidly restored after re-adhesion to the ECM protein fibronectin, suggesting a rapidly reversible mode of regulation. Furthermore, the loss of Nck binding correlates with changes in the phosphorylation state of PAK in non-adherent cells, as evidenced by electrophoretic mobility shift and phosphorylation within a sequence known to mediate interaction with Nck. The ability of cell adhesion to regulate PAK phosphorylation and interaction with Nck may contribute to the anchorage-dependence of PAK activation, as well as the localization of activated PAK within a cell.
J. Biol. Chem, 10.1074/jbc.C000797200
Submitted on November 9, 2000
Revised on March 6, 2001
Accepted on March 13, 2001
Cell adhesion regulates the interaction between Nck and p21-activated kinase
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