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Vol. 14, Issue 3, 973-986, March 2003
Insulin stimulates glucose transport in fat and muscle cells by
triggering exocytosis of the glucose transporter GLUT4. To define the
intracellular trafficking of GLUT4, we have studied the internalization
of an epitope-tagged version of GLUT4 from the cell surface. GLUT4
rapidly traversed the endosomal system en route to a perinuclear
location. This perinuclear GLUT4 compartment did not colocalize with
endosomal markers (endosomal antigen 1 protein, transferrin) or
TGN38, but showed significant overlap with the TGN target (t)-soluble
N-ethylmaleimide-sensitive factor attachment protein
receptors (SNAREs) Syntaxins 6 and 16. These results were confirmed by
vesicle immunoisolation. Consistent with a role for Syntaxins 6 and 16 in GLUT4 trafficking we found that their expression was up-regulated
significantly during adipocyte differentiation and insulin stimulated
their movement to the cell surface. GLUT4 trafficking between endosomes
and trans-Golgi network was regulated via an acidic
targeting motif in the carboxy terminus of GLUT4, because a mutant
lacking this motif was retained in endosomes. We conclude that GLUT4 is
rapidly transported from the cell surface to a subdomain of the
trans-Golgi network that is enriched in the t-SNAREs
Syntaxins 6 and 16 and that an acidic targeting motif in the C-terminal
tail of GLUT4 plays an important role in this process.
Institute for Molecular Biosciences and
Department of Physiology and Pharmacology,
University of Queensland, St. Lucia, Brisbane, QLD 4072, Australia;
§Garvan Institute of Medical Research, St.
Vincent's Hospital, Darlinghurst, 2010 New South Wales, Australia; and
Membrane Biology Laboratory, Institute of
Molecular and Cell Biology, National University of Singapore, Singapore
117609
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