Regulation of insulin receptor function |
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Authors: | J F Youngren |
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Institution: | (1) Mount Zion Medical Center, Diabetes and Endocrine Research, University of California at San Francisco, San Francisco, CA 94143-1616, USA |
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Abstract: | 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.
Received 3 August 2006; received after revision 1 December 2006; accepted 8 January 2007 |
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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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