FCCC LOGO Faculty Publications
Bokoch GM , Wang Y , Bohl BP , Sells MA , Quilliam LA , Knaus UG
Interaction of the Nck adapter protein with p21-activated kinase (PAK1)
Journal of Biological Chemistry. 1996 Oct 18;271(42) :25746-25749
PMID: ISI:A1996VN18000007   
Back to previous list
The p21-activated kinases (PAKs) link G protein-coupled receptors and growth factor receptors (S. Dharmawardhane, R. H. Daniels, and G. M. Bokoch, submitted for publication) to activation of MAP kinase cascades and to cytoskeletal reorganization (M. A. Sells, U. G. Knaus, D. Ambrose, S. Bagrodia, G. M. Bokoch, and J. Chernoff, submitted for publication), The proteins that interact with PAK to mediate its cellular effects and to couple it to upstream receptors are unknown, We describe here a specific interaction of the Nck adapter molecule with PAK1 both in vitro and in vivo. PAK1 and Nck associate in COS-7 and Swiss 3T3 cells constitutively, but this interaction is strengthened upon platelet-derived growth factor receptor stimulation. We show that Nck binds to PAK1 through its second Src homology 3 (SH3) domain, while PAK1 interacts with Nck via the first proline-rich SH3 binding motif at its amino terminus. The interaction of active PAK1 with Nck leads to the phosphorylation of Nck at multiple sites, Association of Nck with PAK1 may serve to link this important regulatory kinase to cell activation by growth factor receptors.
Times Cited: 132 English Article VN180 J BIOL CHEM