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Papers In Press, published online ahead of print July 12, 2002
J. Biol. Chem, 10.1074/jbc.C200383200
Submitted on July 1, 2002
Revised on July 11, 2002
Accepted on July 12, 2002
12, but not G13 to lipid rafts
NIH, Bethesda, MD 20817
Corresponding Author: tlzj{at}helix.nih.gov
The heterotrimeric G proteins, G{sub12} and G{sub13}, are closely related in their sequences, signaling partners and cellular effects such as oncogenic transformation and cytoskeletal reorganization. Yet, G{sub12} and G{sub13} can act through different pathways, bind different proteins and show opposing actions on some effectors. We investigated the compartmentalization of G{sub12} and G{sub13} 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. G
12 was in the lipid raft fractions, whereas G13 was not associated with lipid rafts. Mutation of C11 on G12, which prevents its palmitoylation, partially shifted G12 from the lipid rafts. Geldanamycin treatment, which specifically inhibits Hsp90, caused a partial loss of wild-type G12 and a complete loss of the C11 mutant from the lipid rafts and the appearance of a higher molecular weight form of G12 in the soluble fractions. These results indicate that acylation and Hsp90 interactions localized G12 to lipid rafts. Hsp90 may act as both a scaffold and chaperone to maintain a functional G12 only in discrete membrane domains and thereby explain some of the nonoverlapping functions of G{sub12} and G{sub13} and control of these potent cell regulators.
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