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Originally published In Press as doi:10.1074/jbc.M000415200 on March 15, 2000
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J Biol Chem, Vol. 275, Issue 20, 14992-14999, May 19, 2000

Galpha 13 Requires Palmitoylation for Plasma Membrane Localization, Rho-dependent Signaling, and Promotion of p115-RhoGEF Membrane Binding*

Raja Bhattacharyya and Philip B. WedegaertnerDagger

From the Department of Microbiology and Immunology and Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107

Most heterotrimeric G protein alpha  subunits are covalently modified by palmitate attached to one or more N-terminal cysteine residues. Although a wide variety of proteins undergo palmitoylation, the role of this fatty acid modification in G protein signaling is not well understood. Thus, we examined the role of palmitoylation of alpha 13, a G protein alpha  subunit that regulates many pathways involved in cell growth. Both N-terminal cysteines at positions 14 and 18 were required for palmitoylation. Mutant alpha 13, in which both cysteines were changed to serines, failed to localize to plasma membranes in transfected cells and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. However, nonpalmitoylated, cysteine to serine mutant alpha 13 retained the ability to co-immunoprecipitate with a direct effector, p115-RhoGEF. Finally, we report the novel observation that activated alpha 13 induces a redistribution of p115-RhoGEF from the cytoplasm to plasma membranes, but non-palmitoylated mutants of alpha 13 fail to cause p115-RhoGEF translocation. These findings identify palmitoylation of alpha 13 as critical for its proper membrane localization and signaling and provide insight into the mechanism of activation of Rho-dependent signaling pathways by alpha 13.

* This work was supported in part by a grant from the W. W. Smith Charitable Trust (to P. B. W.) and by National Institutes of Health Grant GM56444 (to P. B. W.).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.

Dagger Pew Scholar in the Biomedical Sciences. To whom correspondence should be addressed: Dept. of Microbiology and Immunology, Kimmel Cancer Institute, Thomas Jefferson University, 233 S. 10th St., 839 BLSB, Philadelphia, PA 19107. Tel.: 215-503-3137; Fax: 215-923-2117; E-mail: P_Wedegaertner@lac.jci.tju.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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