Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 64, Issue 7-8, Pages 873-891Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-007-6359-9
Keywords
tyrosine kinase; autophosphorylation; insulin resistance; ectonucleotide pyrophosphatase phosphodiesterase 1; PC-1; suppressor of cytokine signaling; protein kinase C; tyrosine phosphatise
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Resistance to the biological actions of insulin contributes to the development of type 2 diabetes and risk of cardiovascular disease. A reduced biological response to insulin by tissues results from an impairment in the cascade of phosphorylation events within cells that regulate the activity of enzymes comprising the insulin signaling pathway. In most models of insulin resistance, there is evidence that this decrement in insulin signaling begins with either the activation or substrate kinase activity of the insulin receptor (IR), which is the only component of the pathway that is unique to insulin action. Activation of the IR can be impaired by post-translational modifications of the protein involving serine phosphorylation, or by binding to inhibiting proteins such as PC-1 or members of the SOCS or Grb protein families. The impact of these processes on the conformational changes and phosphorylation events required for full signaling activity, as well as the role of these mechanisms in human disease, is reviewed in this article.
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