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Papers In Press, published online ahead of print November 3, 2000
J. Biol. Chem, 10.1074/jbc.M007231200
Submitted on August 9, 2000
Revised on November 1, 2000
Accepted on November 3, 2000

PKC-zeta phosphorylates IRS-1 and impairs its ability to activate PI 3-kinase in response to insulin

Lingamanaidu V. Ravichandran, Diana L. Esposito, Judy Chen, and Michael J. Quon

Cardiology Branch, NHLBI, National Institutes of Health, Bethesda, MD 20892-1755

Corresponding Author: quonm{at}nih.gov

PKC-zeta is a serine-threonine kinase downstream from PI 3-kinase in insulin signaling pathways. However, specific substrates for PKC-zeta that participate in biological actions of insulin have not been reported. In the present study, we identified IRS-1 as a novel substrate for PKC-zeta . Under in vitro conditions, wild-type PKC-zeta (but not kinase-deficient mutant PKC-zeta ) significantly phosphorylated IRS-1. This phosphorylation was reversed by treatment with the serine-specific phosphatase PP-2A. In addition, overexpression of PKC-zeta in NIH-3T3IR cells caused significant phosphorylation of co-transfected IRS-1 as demonstrated by [32P]-orthophosphate labeling experiments. In rat adipose cells, endogenous IRS-1 co-immunoprecipitated with endogenous PKC-zeta and this association was increased 2-fold upon insulin stimulation. Furthermore, overexpression of PKC-zeta in NIH-3T3IR cells significantly impaired insulin-stimulated tyrosine phosphorylation of co-transfected IRS-1. Importantly, this was accompanied by impaired IRS-1-associated PI 3-kinase activity. Taken together, our results raise the possibility that IRS-1 is a novel physiological substrate for PKC-zeta . Since PKC-zeta is located downstream from IRS-1 and PI 3-kinase in established insulin signaling pathways, PKC-zeta may participate in negative feedback pathways to IRS-1 similar to those previously described for Akt and GSK-3.


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