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J. Biol. Chem., Vol. 276, Issue 9, 6065-6068, March 2, 2001
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From the In adipose and muscle, insulin stimulates
glucose uptake and glycogen synthase activity. Phosphatidylinositol
3-kinase (PI3K) activation is necessary but not sufficient for these
metabolic actions of insulin. The insulin-stimulated translocation of
phospho-c-Cbl to lipid rafts, via its association with CAP, comprises a
second pathway regulating GLUT4 translocation. In 3T3-L1 adipocytes, overexpression of a dominant negative CAP mutant (CAP
ACCELERATED PUBLICATION
Activation of Glycogen Synthase by Insulin in 3T3-L1 Adipocytes
Involves c-Cbl-associating Protein (CAP)-dependent and
CAP-independent Signaling Pathways*
§¶,§
Departments of Medicine and Physiology,
University of Michigan, Ann Arbor, Michigan 48109 and the
§ Department of Cell Biology, Pfizer Global Research and
Development, Ann Arbor, Michigan 48105
SH3) completely blocked the insulin-stimulated glucose transport and glycogen synthesis
but only partially inhibited glycogen synthase activation. In contrast,
CAPSH3 expression did not affect glycogen synthase activation by
insulin in the absence of extracellular glucose. Moreover, CAPSH3
has no effect on the PI3K-dependent activation of protein
phosphatase-1 or phosphorylation of glycogen synthase kinase-3. These
results indicate blockade of the c-Cbl/CAP pathway directly inhibits
insulin-stimulated glucose uptake, which results in secondary
inhibition of glycogen synthase activation and glycogen synthesis.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: University of
Michigan Medical Center, MSRB I, Rm. 4520, 1150 West Medical Center Dr., Ann Arbor, MI 48109. Tel.: 734-615-9787; Fax: 734-936-2888; E-mail: saltiel@umich.edu.
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