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Originally published In Press as doi:10.1074/jbc.C200383200 on July 12, 2002

J. Biol. Chem., Vol. 277, Issue 36, 32409-32412, September 6, 2002
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ACCELERATED PUBLICATION
Hsp90 Interactions and Acylation Target the G Protein Galpha 12 but Not Galpha 13 to Lipid Rafts*

Abdul A. Waheed and Teresa L. Z. JonesDagger

From the Metabolic Diseases Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892

The heterotrimeric G proteins, G12 and G13, are closely related in their sequences, signaling partners, and cellular effects such as oncogenic transformation and cytoskeletal reorganization. Yet G12 and G13 can act through different pathways, bind different proteins, and show opposing actions on some effectors. We investigated the compartmentalization of G12 and G13 at the membrane because other G proteins reside in lipid rafts, membrane microdomains enriched in cholesterol and sphingolipids. Lipid rafts were isolated after cold, nonionic detergent extraction of cells and gradient centrifugation. Galpha 12 was in the lipid raft fractions, whereas Galpha 13 was not associated with lipid rafts. Mutation of Cys-11 on Galpha 12, which prevents its palmitoylation, partially shifted Galpha 12 from the lipid rafts. Geldanamycin treatment, which specifically inhibits Hsp90, caused a partial loss of wild-type Galpha 12 and a complete loss of the Cys-11 mutant from the lipid rafts and the appearance of a higher molecular weight form of Galpha 12 in the soluble fractions. These results indicate that acylation and Hsp90 interactions localized Galpha 12 to lipid rafts. Hsp90 may act as both a scaffold and chaperone to maintain a functional Galpha 12 only in discrete membrane domains and thereby explain some of the nonoverlapping functions of G12 and G13 and control of these potent cell regulators.

* 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 To whom correspondence should be addressed: National Institutes of Health, Bldg. 10/Rm. 9C101, Bethesda, MD 20892-1802. E-mail: tlzj@helix.nih.gov.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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