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J Biol Chem, Vol. 274, Issue 14, 9351-9356, April 2, 1999
From the Department of Molecular Pharmacology, Stanford University
School of Medicine, Stanford, California 94305
Serine/threonine phosphorylation of insulin
receptor substrate 1 (IRS-1) has been implicated as a negative
regulator of insulin signaling. Prior studies have indicated that this
negative regulation by protein kinase C involves the mitogen-activated
protein kinase and phosphorylation of serine 612 in IRS-1. In the
present studies, the negative regulation by platelet-derived growth
factor (PDGF) was compared with that induced by endothelin-1, an
activator of protein kinase C. In contrast to endothelin-1, the
inhibitory effects of PDGF did not require mitogen-activated protein
kinase or the phosphorylation of serine 612. Instead, three other
serines in the phosphorylation domain of IRS-1 (serines 632, 662, and 731) were required for the negative regulation by PDGF. In addition, the PDGF-activated serine/threonine kinase called Akt was found to
inhibit insulin signaling. Moreover, this inhibition required the same
IRS-1 serine residues as the inhibition by PDGF. Finally, the negative
regulatory effects of PDGF and Akt were inhibited by rapamycin, an
inhibitor of the mammalian target of rapamycin (mTOR), one of the
downstream targets of Akt. These studies implicate the
phosphatidylinositol 3-kinase/Akt kinase cascade as an additional negative regulatory pathway for the insulin signaling cascade.
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