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Vol. 11, Issue 7, 2403-2417, July 2000
and§
*Programme in Cell Biology, The Hospital for Sick Children,
Toronto, Ontario M5G 1X8, Canada; Like neuronal synaptic vesicles, intracellular GLUT4-containing
vesicles must dock and fuse with the plasma membrane, thereby facilitating insulin-regulated glucose uptake into muscle and fat
cells. GLUT4 colocalizes in part with the vesicle SNAREs VAMP2 and
VAMP3. In this study, we used a single-cell fluorescence-based assay to
compare the functional involvement of VAMP2 and VAMP3 in GLUT4
translocation. Transient transfection of proteolytically active tetanus
toxin light chain cleaved both VAMP2 and VAMP3 proteins in L6 myoblasts
stably expressing exofacially myc-tagged GLUT4 protein and inhibited
insulin-stimulated GLUT4 translocation. Tetanus toxin also caused
accumulation of the remaining C-terminal VAMP2 and VAMP3 portions in
Golgi elements. This behavior was exclusive to these proteins, because
the localization of intracellular myc-tagged GLUT4 protein was not
affected by the toxin. Upon cotransfection of tetanus toxin with
individual vesicle SNARE constructs, only toxin-resistant VAMP2 rescued
the inhibition of insulin-dependent GLUT4 translocation by tetanus
toxin. Moreover, insulin caused a cortical actin filament
reorganization in which GLUT4 and VAMP2, but not VAMP3, were clustered.
We propose that VAMP2 is a resident protein of the insulin-sensitive
GLUT4 compartment and that the integrity of this protein is required
for GLUT4 vesicle incorporation into the cell surface in response to insulin.
Department of
Biochemistry, University of Toronto, Toronto, Ontario M5G 1AS, Canada;
and Institut de Biologie Cellulaire et de Morphologie,
University of Lausanne, Lausanne, Switzerland
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