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J Biol Chem, Vol. 274, Issue 44, 31641-31647, October 29, 1999

Reciprocal Signaling between Heterotrimeric G Proteins and the p21-stimulated Protein Kinase

Jun Wang, Jeffrey A. Frost, Melanie H. Cobb, and Elliott M. Ross

From the Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9041

p21-activated protein kinase (PAK)-1 phosphorylated Galpha z, a member of the Galpha i family that is found in the brain, platelets, and adrenal medulla. Phosphorylation approached 1 mol of phosphate/mol of Galpha z in vitro. In transfected cells, Galpha z was phosphorylated both by wild-type PAK1 when stimulated by the GTP-binding protein Rac1 and by constitutively active PAK1 mutants. In vitro, phosphorylation occurred only at Ser16, one of two Ser residues that are the major substrate sites for protein kinase C (PKC). PAK1 did not phosphorylate other Galpha subunits (i1, i2, i3, o, s, or q). PAK1-phosphorylated Galpha z was resistant both to RGSZ1, a Gz-selective GTPase-activating protein (GAP), and to RGS4, a relatively nonselective GAP for the Gi and Gq families of G proteins. Phosphorylation of Ser27 by PKC did not alter sensitivity to either GAP. The previously described inhibition of Gz GAPs by PKC is therefore mediated by phosphorylation of Ser16. Phosphorylation of either Ser16 by PAK1 or Ser27 by PKC decreased the affinity of Galpha z for Gbeta gamma ; phosphorylation of both residues by PKC caused no further effect. PAK1 thus regulates Galpha z function by attenuating the inhibitory effects of both GAPs and Gbeta gamma . In this context, the kinase activity of PAK1 toward several protein substrates was directly inhibited by Gbeta gamma , suggesting that PAK1 acts as a Gbeta gamma -regulated effector protein. This inhibition of mammalian PAK1 by Gbeta gamma contrasts with the stimulation of the PAK homolog Ste20p in Saccharomyces cerevisiae by the Gbeta gamma homolog Ste4p/Ste18p.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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