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Vol. 273, Issue 3, 1444-1452, January 16, 1998
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From the Vesicle-associated membrane protein 2 (VAMP2) has
been implicated in the insulin-regulated trafficking of GLUT4 in
adipocytes. It has been proposed that VAMP2 co-localizes with GLUT4 in
a postendocytic storage compartment (Martin, S., Tellam, J.,
Livingstone, C., Slot, J. W., Gould, G. W., and James,
D. E. (1996) J. Cell Biol. 134, 625-635), suggesting
that it may play a role distinct from endosomal v-SNAREs (soluble
N-ethylmaleimide-sensitive factor attachment protein
receptors) such as cellubrevin that are also expressed in adipocytes.
The present study examines the effects of recombinant glutathione
S-transferase (GST) fusion proteins encompassing the entire
cytoplasmic tails of VAMP1, VAMP2, and cellubrevin on
insulin-stimulated GLUT4 translocation in streptolysin O permeabilized
3T3-L1 adipocytes. GST-VAMP2 inhibited insulin-stimulated GLUT4
translocation by ~35%, whereas GST-VAMP1 and GST-cellubrevin were
without effect. A synthetic peptide corresponding to the unique N
terminus of VAMP2 also inhibited insulin-stimulated GLUT4 translocation
in a dose-dependent manner. This peptide had no effect on
either guanosine 5 Centre for Molecular and Cellular Biology
and Department of Physiology and Pharmacology, University of
Queensland, St. Lucia 4072, Australia and the § Division of
Biochemistry and Molecular Biology, University of Glasgow,
Glasgow G12 8QQ, Scotland
-3-O-(thio)triphosphate-stimulated GLUT4
translocation or on insulin-stimulated GLUT1 translocation. These
results imply that GLUT4 and GLUT1 may undergo insulin-stimulated translocation to the cell surface from separate intracellular compartments. To confirm this, adipocytes were incubated with a
transferrin-horseradish peroxidase conjugate to fill the itinerant endocytic system after which cells were incubated with
H2O2 and diaminobenzidine. This treatment
completely blocked insulin-stimulated movement of GLUT1, whereas in the
case of GLUT4, movement to the surface was delayed but still reached
similar levels to that observed in insulin-stimulated control cells
after 30 min. These results suggest that the N terminus of VAMP2 plays
a unique role in the insulin-dependent recruitment of GLUT4
from its intracellular storage compartment to the cell surface.
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