Insulin modulates many intracellular processes including cellular metabolism, cell proliferation and cell differentiation. Some of these processes involve significant changes in the traffic of intracellular vesicles or in the structural organization of the cell. These phenomena have been linked to the activity of regulatory GTP-binding proteins. Most, if not all functions, of the insulin receptor are associated with its tyrosine kinase activity. Thus, over the past few years, a significant effort has been dedicated to elucidate the cross-talk between the tyrosine kinase activity of the receptor and the regulation of G protein-mediated pathways. Recent progress indicates that G proteins may mediate the control of several of insulin's intracellular functions. These include the regulation of the MAP kinase pathway, the activation of phospholipase D and the regulation of glucose uptake. This article discusses some recent advances in this area.
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Rizzo et al. (1998) studied this question.
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