Chapter 12 Serine Kinases of Insulin Receptor Substrate Proteins

Author(s):  
Sigalit Boura‐Halfon ◽  
Yehiel Zick
2009 ◽  
Vol 7 (1) ◽  
pp. 14 ◽  
Author(s):  
Katerina Mardilovich ◽  
Shannon L Pankratz ◽  
Leslie M Shaw

2001 ◽  
Vol 15 (11) ◽  
pp. 1864-1869 ◽  
Author(s):  
Gerasimos P. Sykiotis ◽  
Athanasios G. Papavassiliou

Abstract Insulin resistance, the failure to respond to normal circulating concentrations of insulin, is a common state associated with obesity, aging, and a sedentary lifestyle. Compelling evidence implicates TNFα as the cause and link between obesity and insulin resistance. Serine phosphorylation of insulin receptor substrate-1 seems prominent among the mechanisms of TNFα-induced insulin resistance. Recent advances indicate that serine kinases may phosphorylate and thus inhibit the tyrosine phosphorylation of insulin receptor substrate-1, revealing an integration point of TNFα and insulin signaling pathways. Selective targeting of the molecular scenery whereby this key phosphorylation occurs/operates represents a rich area for the development of rationally designed new antidiabetic drugs. In relation to efficacy and side effects, this prospect should permit a more precise and perhaps individualized approach to therapeutic intervention, allowing clinicians to focus the attack where the problem lies.


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