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J Biol Chem, Vol. 275, Issue 3, 2191-2198, January 21, 2000
From the Domains rich in sphingolipids and cholesterol, or
rafts, may organize signal transduction complexes at the plasma
membrane. Raft lipids are believed to exist in a state similar to the
liquid-ordered phase. It has been proposed that proteins with a high
affinity for an ordered lipid environment will preferentially partition into rafts (Melkonian, K. A., Ostermeyer, A. G., Chen,
J. Z., Roth, M. G., and Brown, D. A. (1999)
J. Biol. Chem. 274, 3910-3917). We investigated the
possibility that lipid-lipid interactions between lipid-modified
proteins and raft lipids mediate targeting of proteins to these
domains. G protein monomers or trimers were reconstituted in liposomes,
engineered to mimic raft domains. Assay for partitioning of G proteins
into rafts was based on Triton X-100 insolubility. Myristoylation and
palmitoylation of G
Lipid-dependent Targeting of G Proteins into
Rafts*
,¶
Department of Cell Biology and Physiology,
Washington University School of Medicine, St. Louis, Missouri 63110 and the § Department of Biochemistry and Cell Biology, State
University of New York, Stony Brook, New York 11794-5215
i were necessary and sufficient for
association with liposomes and partitioning into rafts. Strikingly, the
amount of fatty-acylated Gi in rafts was significantly
reduced when myristoylated Gi was thioacylated with
cis-unsaturated fatty acids instead of saturated fatty
acids such as palmitate. Prenylated 
subunits were excluded from
rafts, whether reconstituted alone or with fatty-acylated subunits. These results suggest that the structural difference between lipids that modify proteins is one basis for the selectivity of protein targeting to rafts.
*
This work was supported by a postdoctoral fellowship from
the Missouri affiliate of the American Heart Association (to S. M.) and National Institutes of Health Grants GM51466 (to M. E. L.) and GM47897 (to D. A. B.).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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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C. Blanpain, V. Wittamer, J.-M. Vanderwinden, A. Boom, B. Renneboog, B. Lee, E. Le Poul, L. El Asmar, C. Govaerts, G. Vassart, et al. Palmitoylation of CCR5 Is Critical for Receptor Trafficking and Efficient Activation of Intracellular Signaling Pathways J. Biol. Chem., June 22, 2001; 276(26): 23795 - 23804. [Abstract] [Full Text] [PDF]
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X. Liang, A. Nazarian, H. Erdjument-Bromage, W. Bornmann, P. Tempst, and M. D. Resh Heterogeneous Fatty Acylation of Src Family Kinases with Polyunsaturated Fatty Acids Regulates Raft Localization and Signal Transduction J. Biol. Chem., August 10, 2001; 276(33): 30987 - 30994. [Abstract] [Full Text] [PDF]
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X. Xu, R. Bittman, G. Duportail, D. Heissler, C. Vilcheze, and E. London Effect of the Structure of Natural Sterols and Sphingolipids on the Formation of Ordered Sphingolipid/Sterol Domains (Rafts). COMPARISON OF CHOLESTEROL TO PLANT, FUNGAL, AND DISEASE-ASSOCIATED STEROLS AND COMPARISON OF SPHINGOMYELIN, CEREBROSIDES, AND CERAMIDE J. Biol. Chem., August 31, 2001; 276(36): 33540 - 33546. [Abstract] [Full Text] [PDF]
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T. M. Stulnig, J. Huber, N. Leitinger, E.-M. Imre, P. Angelisova, P. Nowotny, and W. Waldhausl Polyunsaturated Eicosapentaenoic Acid Displaces Proteins from Membrane Rafts by Altering Raft Lipid Composition J. Biol. Chem., September 28, 2001; 276(40): 37335 - 37340. [Abstract] [Full Text] [PDF]
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D. A. Brown and E. London Structure and Function of Sphingolipid- and Cholesterol-rich Membrane Rafts J. Biol. Chem., June 2, 2000; 275(23): 17221 - 17224. [Full Text] [PDF]
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I. Rousso, M. B. Mixon, B. K. Chen, and P. S. Kim Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity PNAS, December 5, 2000; 97(25): 13523 - 13525. [Abstract] [Full Text] [PDF]
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 S. X. Lu and E. M. Hrabak An Arabidopsis Calcium-Dependent Protein Kinase Is Associated with the Endoplasmic Reticulum Plant Physiology, March 1, 2002; 128(3): 1008 - 1021. [Abstract] [Full Text] [PDF]
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