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J Biol Chem, Vol. 274, Issue 53, 38260-38267, December 31, 1999

Palmitoylation of a Conserved Cysteine in the Regulator of G Protein Signaling (RGS) Domain Modulates the GTPase-activating Activity of RGS4 and RGS10*

Yaping TuDagger , Sergei PopovDagger , Clive Slaughter§, and Elliott M. RossDagger

From the Departments of Dagger  Pharmacology and § Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9041

RGS4 and RGS10 expressed in Sf9 cells are palmitoylated at a conserved Cys residue (Cys95 in RGS4, Cys66 in RGS10) in the regulator of G protein signaling (RGS) domain that is also autopalmitoylated when the purified proteins are incubated with palmitoyl-CoA. RGS4 also autopalmitoylates at a previously identified cellular palmitoylation site, either Cys2 or Cys12. The C2A/C12A mutation essentially eliminates both autopalmitoylation and cellular [3H]palmitate labeling of Cys95. Membrane-bound RGS4 is palmitoylated both at Cys95 and Cys2/12, but cytosolic RGS4 is not palmitoylated. RGS4 and RGS10 are GTPase-activating proteins (GAPs) for the Gi and Gq families of G proteins. Palmitoylation of Cys95 on RGS4 or Cys66 on RGS10 inhibits GAP activity 80-100% toward either Galpha i or Galpha z in a single-turnover, solution-based assay. In contrast, when GAP activity was assayed as acceleration of steady-state GTPase in receptor-G protein proteoliposomes, palmitoylation of RGS10 potentiated GAP activity >= 20-fold. Palmitoylation near the N terminus of C95V RGS4 did not alter GAP activity toward soluble Galpha z and increased Gz GAP activity about 2-fold in the vesicle-based assay. Dual palmitoylation of wild-type RGS4 remained inhibitory. RGS protein palmitoylation is thus multi-site, complex in its control, and either inhibitory or stimulatory depending on the RGS protein and its sites of palmitoylation.

* This work was supported by National Institutes of Health Grant GM30355 and Welch Foundation Grant I-0982 (to E. M. R.) and R. A. Welch Foundation Grant I-1382 (to Thomas M. Wilkie, this department).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9041. Tel.: 214-648-8717; Fax: 214-648-2994; E-mail: ross@utsw.swmed.edu.

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