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Published online
doi:10.1083/jcb.200709108
The Journal of Cell Biology, Vol. 180, No. 2, 375-387
The Rockefeller University Press, 0021-9525 $30.00
© Williams et al.
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Article

Mapping of R-SNARE function at distinct intracellular GLUT4 trafficking steps in adipocytes



Dumaine Williams and Jeffrey E. Pessin

Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY 11794

Correspondence to Jeffrey E. Pessin: pessin{at}pharm.stonybrook.edu

The functional trafficking steps used by soluble NSF attachment protein receptor (SNARE) proteins have been difficult to establish because of substantial overlap in subcellular localization and because in vitro SNARE-dependent binding and fusion reactions can be promiscuous. Therefore, to functionally identify the site of action of the vesicle-associated membrane protein (VAMP) family of R-SNAREs, we have taken advantage of the temporal requirements of adipocyte biosynthetic sorting of a dual-tagged GLUT4 reporter (myc-GLUT4-GFP) coupled with small interfering RNA gene silencing. Using this approach, we confirm the requirement of VAMP2 and VAMP7 for insulin and osmotic shock trafficking from the vesicle storage sites, respectively, and fusion with the plasma membrane. Moreover, we identify a requirement for VAMP4 for the initial biosynthetic entry of GLUT4 from the Golgi apparatus into the insulin-responsive vesicle compartment, VAMP8, for plasma membrane endocytosis and VAMP2 for sorting to the specialized insulin-responsive compartment after plasma membrane endocytosis.

Abbreviations used in this paper: ANOVA, analysis of variance; VAMP, vesicle-associated membrane protein.


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