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Volume 270, Number 47, Issue of November 24, 1995 pp. 27991-27994
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Insulin-stimulated GLUT4 Translocation Is Mediated by a Divergent Intracellular Signaling Pathway

(Received for publication, August 1, 1995; and in revised form, September 25, 1995)

Tetsuro Haruta,  Aaron J. Morris,  David W. Rose,  James G. Nelson ,  Michael Mueckler ,  Jerrold M. Olefsky

Insulin stimulates glucose transport largely by mediating translocation of the insulin-sensitive glucose transporter (GLUT4) from an intracellular compartment to the plasma membrane. Using single cell microinjection of 3T3-L1 adipocytes, coupled with immunofluorescence detection of GLUT4 proteins, we have determined that inhibition of endogenous p21 or injection of oncogenic p21 has no effect on insulin-stimulated GLUT4 translocation. On the other hand, microinjection of anti-phosphotyrosine antibodies or inhibition of endogenous phosphatidylinositol 3-kinase by microinjection of a GST-p85 SH2 fusion protein markedly inhibits this biologic effect of insulin. These data suggest that the p21/mitogen-activated protein kinase pathway is not involved in this metabolic effect of insulin, whereas tyrosine phosphorylation and stimulation of phosphatidylinositol 3-kinase activity are critical components of this signaling pathway.



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