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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Haruta, T. et al.

Insulin-stimulated GLUT4 translocation is mediated by a divergent intracellular signaling pathway.

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 p21ras or injection of oncogenic p21ras 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 p21ras/ 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.[1]

References

Insulin-stimulated GLUT4 translocation is mediated by a divergent intracellular signaling pathway. Haruta, T., Morris, A.J., Rose, D.W., Nelson, J.G., Mueckler, M., Olefsky, J.M. J. Biol. Chem. (1995) [Pubmed]

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