Differential regulation of secretory compartments containing the insulin-responsive glucose transporter in 3T3-L1 adipocytes

Millar, Caroline A., Shewan, Annette M., Hickson, Gilles R. X., James, David E. and Gould, Gwyn W. (1999) Differential regulation of secretory compartments containing the insulin-responsive glucose transporter in 3T3-L1 adipocytes. Molecular Biology of the Cell, 10 11: 3675-3688.

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Author Millar, Caroline A.
Shewan, Annette M.
Hickson, Gilles R. X.
James, David E.
Gould, Gwyn W.
Title Differential regulation of secretory compartments containing the insulin-responsive glucose transporter in 3T3-L1 adipocytes
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 1999-11
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 10
Issue 11
Start page 3675
End page 3688
Total pages 14
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Collection year 1999
Language eng
Abstract Insulin and guanosine-5'-O-(3-thiotriphosphate) (GTPgamma S) both stimulate glucose transport and translocation of the insulin-responsive glucose transporter 4 (GLUT4) to the plasma membrane in adipocytes. Previous studies suggest that these effects may be mediated by different mechanisms. In this study we have tested the hypothesis that these agonists recruit GLUT4 by distinct trafficking mechanisms, possibly involving mobilization of distinct intracellular compartments. We show that ablation of the endosomal system using transferrin-HRP causes a modest inhibition (~30%) of insulin-stimulated GLUT4 translocation. In contrast, the GTPgamma S response was significantly attenuated (~85%) under the same conditions. Introduction of a GST fusion protein encompassing the cytosolic tail of the v-SNARE cellubrevin inhibited GTPgamma S-stimulated GLUT4 translocation by ~40% but had no effect on the insulin response. Conversely, a fusion protein encompassing the cytosolic tail of vesicle-associated membrane protein-2 had no significant effect on GTPgamma S-stimulated GLUT4 translocation but inhibited the insulin response by ~40%. GTPgamma S- and insulin-stimulated GLUT1 translocation were both partially inhibited by GST-cellubrevin (~50%) but not by GST-vesicle-associated membrane protein-2. Incubation of streptolysin O-permeabilized 3T3-L1 adipocytes with GTPgamma S caused a marked accumulation of Rab4 and Rab5 at the cell surface, whereas other Rab proteins (Rab7 and Rab11) were unaffected. These data are consistent with the localization of GLUT4 to two distinct intracellular compartments from which it can move to the cell surface independently using distinct sets of trafficking molecules.
Q-Index Code C1
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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Created: Tue, 10 Jun 2008, 15:06:05 EST