[HTML][HTML] Protein kinase C θ inhibits insulin signaling by phosphorylating IRS1 at Ser1101
Y Li, TJ Soos, X Li, J Wu, M DeGennaro, X Sun… - Journal of Biological …, 2004 - ASBMB
Obesity and stress inhibit insulin action by activating protein kinases that enhance serine
phosphorylation of IRS1 and have been thus associated to insulin resistance and the
development of type II diabetes. The protein kinase C θ (PKCθ) is activated by free-fatty
acids, and its activity is higher in muscle from obese diabetic patients. However, a molecular
link between PKCθ and insulin resistance has not been defined yet. Here we show that
PKCθ phosphorylates IRS1 at serine 1101 blocking IRS1 tyrosine phosphorylation and …
phosphorylation of IRS1 and have been thus associated to insulin resistance and the
development of type II diabetes. The protein kinase C θ (PKCθ) is activated by free-fatty
acids, and its activity is higher in muscle from obese diabetic patients. However, a molecular
link between PKCθ and insulin resistance has not been defined yet. Here we show that
PKCθ phosphorylates IRS1 at serine 1101 blocking IRS1 tyrosine phosphorylation and …