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J. Biol. Chem., Vol. 277, Issue 51, 49750-49754, December 20, 2002
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From the Henry Wellcome Laboratory for Cell Biology, Division of
Biochemistry & Molecular Biology, Davidson Building, Faculty of
Biomedical and Life Sciences, University of Glasgow,
Glasgow G12 8QQ, Scotland, United Kingdom
Insulin stimulates the fusion of intracellular
vesicles containing the glucose transporter Glut4 with the plasma
membrane in adipocytes and muscle cells. Glut4 vesicle fusion is
thought to be catalyzed by the interaction of the vesicle soluble
N-ethyl-maleimide-sensitive fusion protein attachment
protein receptor VAMP2 with the target soluble
N-ethyl-maleimide-sensitive fusion protein attachment protein receptors SNAP-23 and syntaxin 4. Here, we use combined membrane fractionation, detergent solubility, and sucrose gradient flotation to demonstrate that the large majority (>70%) of SNAP-23 and a significant proportion of syntaxin 4 (~35%) are associated with plasma membrane lipid rafts in 3T3-L1 adipocytes. Furthermore, VAMP2 is shown to be concentrated in lipid rafts isolated from intracellular membranes. Insulin stimulation had no effect on the
plasma membrane raft association of SNAP-23 or syntaxin 4 but promoted
VAMP2 insertion into plasma membrane rafts. Immunofluorescence analysis
revealed that SNAP-23 was clustered at the plasma membrane and almost
completely segregated from the transferrin receptor. SNAP-23
distribution seemed to be distinct from caveolin-1, and clusters of
SNAP-23 were dispersed after cholesterol extraction with
methyl-
The Vesicle- and Target-SNARE Proteins That Mediate
Glut4 Vesicle Fusion Are Localized in Detergent-insoluble Lipid Rafts
Present on Distinct Intracellular Membranes*
and
-cyclodextrin, suggesting that the majority of SNAP-23 is
associated with non-caveolar, cholesterol-rich lipid rafts. The results
described implicate lipid rafts as important platforms for Glut4
vesicle fusion and suggest the hypothesis that such rafts may represent
a spatial integration point of insulin signaling and membrane traffic.
*
This work was supported by grants from the Diabetes Research
and Wellness Foundation (fellowship to L. H. C.), Biotechnology and
Biological Sciences Research Council Grant 17/C16435 (to L. H. C. and
G. W. G.), and an equipment grant from the Wellcome Trust (to
G. W. G.).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. Tel.: 44-141-330-2051;
Fax: 44-141-330-4620; E-mail: l.chamberlain@bio.gla.ac.uk.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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