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Insulin activates hexose transport via at least two mechanisms:
a p21
Volume 270,
Number 22,
Issue of June 2, pp. 12965-12968, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-dependent pathway, leading to an increase
in the amount of cell surface GLUT1; and a metabolic,
p21
-independent pathway, leading to
translocation of the insulin-responsive transporter GLUT4 to the cell
surface. Following insulin stimulation, SHPTP2, a non-transmembrane
protein-tyrosine phosphatase, associates with insulin receptor
substrate 1 via its Src homology 2 (SH2) domains. Microinjection of a
glutathione S-transferase fusion protein encoding the N- and
C-terminal SH2 domains of SHPTP2 (GST-NC-SH2) or anti-SHPTP2 antibodies
into NIH-3T3 fibroblasts overexpressing the insulin receptor blocks
insulin-induced DNA synthesis. Microinjection of either GST-NC-SH2 or
anti-SHPTP2 antibodies into 3T3-L1 adipocytes inhibited the
insulin-stimulated increase in expression of GLUT1. In contrast,
translocation of GLUT4 to the cell surface was unaffected by either
GST-NC-SH2 or anti-SHPTP2 antibodies. These data confirm a role for
SHPTP2 in insulin-stimulated mitogenesis and indicate that whereas
SHPTP2 is necessary for insulin-stimulated expression of GLUT1, it is
not required for activation of the metabolic pathway leading to GLUT4
translocation.
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