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Titolo:
The BPS domain of Grb10 inhibits the catalytic activity of the insulin andIGF1 receptors
Autore:
Stein, EG; Gustafson, TA; Hubbard, SR;
Indirizzi:
NYU, Sch Med, Skirball Inst Biomol Med, New York, NY 10016 USA NYU New York NY USA 10016 kirball Inst Biomol Med, New York, NY 10016 USA NYU, Sch Med, Dept Pharmacol, New York, NY 10016 USA NYU New York NY USA 10016 Sch Med, Dept Pharmacol, New York, NY 10016 USA Metabolex Inc, Hayward, CA 94545 USA Metabolex Inc Hayward CA USA 94545Metabolex Inc, Hayward, CA 94545 USA
Titolo Testata:
FEBS LETTERS
fascicolo: 2-3, volume: 493, anno: 2001,
pagine: 106 - 111
SICI:
0014-5793(20010330)493:2-3<106:TBDOGI>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE KINASE DOMAIN; GROWTH-FACTOR RECEPTOR; FACTOR-I RECEPTOR; ADAPTER PROTEIN GRB10; SH2 DOMAIN; PLECKSTRIN HOMOLOGY; CRYSTAL-STRUCTURE; BINDING-PROTEIN; SRC HOMOLOGY-2; IDENTIFICATION;
Keywords:
Grb10; insulin receptor; insulin-like growth factor 1 receptor; receptor tyrosine kinase; enzyme inhibition;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Hubbard, SR NYU, Sch Med, Skirball Inst Biomol Med, 540 1st Ave, New York,NY 10016 USA NYU 540 1st Ave New York NY USA 10016 , New York, NY 10016 USA
Citazione:
E.G. Stein et al., "The BPS domain of Grb10 inhibits the catalytic activity of the insulin andIGF1 receptors", FEBS LETTER, 493(2-3), 2001, pp. 106-111

Abstract

Grb7, Grb10 and Grb14 comprise a family of adaptor proteins that interact with numerous receptor tyrosine kinases upon receptor activation. Between the pleckstrin homology (PH) domain and the Src homology 2 (SH2) domain of these proteins is a region of approximately 50 residues known as the BPS (between PH and SH2) domain. Here we show, using purified recombinant proteins, that the BPS domain of Grb10 directly inhibits substrate phosphorylation by the activated tyrosine kinase domains of the insulin receptor and the insulin-like growth factor I (IGF1) receptor, although inhibition by the BPS domain is dependent on tyrosine phosphorylation of;he kinase activation loop, peptide competition experiments indicate that the BPS domain does not bind directly to phosphotyrosine. These studies pro, ide a molecular mechanism by which Grb10 functions as a negative regulator of insulin- and/or IGF1-mediated signaling, (C) 2001 Published by Elsevier Science B,V, on behalf of the Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/04/20 alle ore 02:39:51