An Insulin Receptor Peptide (1135-1156) Stimulates Guanosine 5'-[gamma-thio]triphosphate Binding to the 67 KDa G-protein Associated with the Insulin Receptor

Overview

Journal Biochem J

Specialty Biochemistry

Date 1993 Aug 15

PMID 8363571

Citations 4

Authors

H Jo

W Radding

G M Anantharamaiah

J M McDonald

Affiliations

Soon will be listed here.

Abstract

Peptides representing two putative G-protein-binding motifs (GPBP1 and GPBP2) derived from insulin-receptor sequences were tested for their ability to stimulate guanosine 5'-[gamma-thio]-triphosphate (GTP[S]; 'GTP gamma S') binding to a preparation containing the 41 and 67 kDa G-proteins that are associated with the insulin receptor [Jo, Cha, Davis and McDonald (1992) Endocrinology (Baltimore) 131, 2855-2861]. GPBP2 (residues 1135-1156) specifically stimulated GTP[S] binding, whereas GPBP1 (1319-1333) did not. Substitution of Arg-1152 with Gln in GPBP2 corresponding to a mutation site in insulin-resistant patients [Cocozza, Porcellini, Riccardi, Monticelli, Condorelli, Ferrera, Pianese, Miele, Capaldo, Beguinot and Varrone (1992) Diabetes 41, 521-526] attenuated the stimulatory potency of GPBP2. Size-exclusion chromatography and studies with purified 67 kDa G-protein revealed that GPBP2 stimulated GTP[S] binding only to the 67 kDa G-protein. These studies provide evidence for a potential regulatory site for G-protein interaction with the insulin receptor in the tyrosine kinase domain.

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