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Titolo:
Human growth factor receptor bound 14 binds the activated insulin receptorand alters the insulin-stimulated tyrosine phosphorylation levels of multiple proteins
Autore:
Hemming, R; Agatep, R; Badiani, K; Wyant, K; Arthur, G; Gietz, RD; Triggs-Raine, B;
Indirizzi:
Univ Manitoba, Dept Biochem & Med Genet, Winnipeg, MB R3E 0W3, Canada UnivManitoba Winnipeg MB Canada R3E 0W3 et, Winnipeg, MB R3E 0W3, Canada
Titolo Testata:
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE
fascicolo: 1, volume: 79, anno: 2001,
pagine: 21 - 32
SICI:
0829-8211(200102)79:1<21:HGFRB1>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
FACTOR-I RECEPTOR; HIGH-EFFICIENCY TRANSFORMATION; SRC HOMOLOGY-2 DOMAIN; SH2 DOMAIN; PLECKSTRIN HOMOLOGY; ESCHERICHIA-COLI; 2-HYBRID SYSTEM; ADAPTER PROTEIN; KINASE DOMAIN; GRB-IR;
Keywords:
insulin signaling; growth factor receptor bound 14; Grb14; adaptor protein; insulin receptor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Triggs-Raine, B Univ Manitoba, Dept Biochem & Med Genet, 770 Bannatyne Ave, Winnipeg, MB R3E 0W3, Canada Univ Manitoba 770 Bannatyne Ave Winnipeg MB Canada R3E 0W3
Citazione:
R. Hemming et al., "Human growth factor receptor bound 14 binds the activated insulin receptorand alters the insulin-stimulated tyrosine phosphorylation levels of multiple proteins", BIOC CELL B, 79(1), 2001, pp. 21-32

Abstract

To identify proteins interacting in the insulin-signaling pathway that might define new pathways or regulate existing ones, we have employed the yeast two-hybrid system. In a two-hybrid screen of a human liver cDNA library, we identified the human growth factor receptor bound 14 (hGrb14) adaptor protein as a partner of the activated insulin receptor. Additional analysis of the insulin receptor - hGrb14 interaction in the yeast two-hybrid system revealed that the SH2 domain of hGrb14 was not the sole region involved in binding the activated insulin receptor. The insulin-stimulated interaction between hGrb14 and the insulin receptor was also observed in different mammalian cultured cell lines. This association was detected at 1 min of insulin stimulation and was maximal at 10 nM and greater concentrations of insulin. Chinese hamster ovary cells stably expressing the insulin receptor (CHO-IR) and hGrb14 were used to examine the effects of hGrb14 overexpression oninsulin-stimulated tyrosine phosphorylation of proteins; in general, increasing levels of hGrb14 expression resulted in a reduction in tyrosine phosphorylation. This decrease was demonstrated for the specific proteins src homology-containing and collagen-related protein (Shc), insulin receptor substrate-1 (IRS-1), and Downstream of tyrosine Kinase (Dok). The broad effectsof hGrb14 overexpression on insulin-stimulated tyrosine phosphorylation suggest that it acts early in the insulin-signaling pathway.

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Documento generato il 30/03/20 alle ore 19:38:52