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J Biol Chem, Vol. 273, Issue 8, 4740-4746, February 20, 1998
, Binds Insulin Receptor
Substrate-1 and Modulates Insulin Signaling
,§, and¶
From the Ottawa Civic Hospital Loeb Research Institute, Ottawa
Civic Hospital, and the Departments of Insulin receptor substrate-1 (IRS-1) is
phosphorylated on multiple tyrosine residues by ligand-activated
insulin receptors. These tyrosine phosphorylation sites serve to dock
several Src homology 2-containing signaling proteins. In addition,
IRS-1 contains a pleckstrin homology domain and a phosphotyrosine
binding domain (PTB) implicated in protein-protein and protein-lipid
interactions. In a yeast two-hybrid screening using Xenopus
IRS-1 (xIRS-1) pleckstrin homology-PTB domains as bait, we identified a
Xenopus homolog of Rho-associated kinase Biochemistry,
§ Medicine, and ¶ Obstetrics and Gynecology, University
of Ottawa, Ottawa K1Y 4E9, Canada
(xROK) as a
potential xIRS-1-binding protein. The original clone contained the
carboxyl terminus of xROK (xROK-C) including the putative Rho
binding domain but lacking the amino-terminal kinase domain. Further
analyses in yeast indicated that xROK-C bound to the putative PTB
domain of xIRS-1. Binding of xROK-C to xIRS-1 was confirmed in
Xenopus oocytes after microinjection of mRNA corresponding
to xROK-C. Furthermore, microinjection of xROK-C mRNA inhibited
insulin-induced mitogen-activated protein kinase activation with a
concomitant inhibition of oocyte maturation. In contrast,
microinjection of xROK-C mRNA did not inhibit mitogen-activated protein
kinase activation or oocyte maturation induced by progesterone or by
microinjection of viral Ras (v-Ras) mRNA. These results suggest that
xROK may play a role in insulin signaling via a direct interaction
with xIRS-1.
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