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Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118
Insulin regulates the uptake of glucose
into skeletal muscle and adipocytes by redistributing the
tissue-specific glucose transporter GLUT4 from intracellular vesicles
to the cell surface. To date, GLUT4 is the only protein involved in
insulin-regulated vesicular traffic that has this tissue distribution,
thus raising the possibility that its expression alone may allow
formation of an insulin-responsive vesicular compartment. We show here
that treatment of differentiating C2C12
myoblasts with dexamethasone, acting via the glucocorticoid receptor,
causes a 
10-fold increase in GLUT4 expression but results in no
significant change in insulin-stimulated glucose transport. Signaling
from the insulin receptor to its target, Akt2, and expression of the
soluble N-ethylmaleimide-sensitive factor-attachment protein
receptor, or SNARE, proteins syntaxin 4 and vesicle-associated membrane
protein are normal in dexamethasone-treated C2C12 cells. However, these cells show no
insulin-dependent trafficking of the insulin-responsive aminopeptidase
or the transferrin receptor, respective markers for intracellular
GLUT4-rich compartments and endosomes that are insulin responsive in
mature muscle and adipose cells. Therefore, these data support the
hypothesis that GLUT4 expression by itself is insufficient to establish
an insulin-sensitive vesicular compartment.
glucocorticoid; skeletal muscle; insulin; glucose transporter; C2C12 cells; protein trafficking
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