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Titolo:
14-3-3-PROTEIN BINDS TO INSULIN-RECEPTOR SUBSTRATE-1, ONE OF THE BINDING-SITES OF WHICH IS IN THE PHOSPHOTYROSINE BINDING DOMAIN
Autore:
OGIHARA T; ISOBE T; ICHIMURA T; TAOKA M; FUNAKI M; SAKODA H; ONISHI Y; INUKAI K; ANAI M; FUKUSHIMA Y; KIKUCHI M; YAZAKI Y; OKA Y; ASANO T;
Indirizzi:
UNIV TOKYO,FAC MED,DEPT INTERNAL MED 3,BUNKYO KU,7-3-1 HONGO TOKYO 113 JAPAN UNIV TOKYO,FAC MED,DEPT INTERNAL MED 3,BUNKYO KU TOKYO 113 JAPAN ASAHI LIFE FDN,INST ADULT DIS,SHINJUKU KU TOKYO 160 JAPAN YAMAGUCHI UNIV,SCH MED,DEPT INTERNAL MED 3 UBE YAMAGUCHI 755 JAPAN TOKYO METROPOLITAN UNIV,FAC SCI,DEPT CHEM HACHIOJI TOKYO 19203 JAPAN NIIGATA UNIV,SCH MED,DEPT CHEM NIIGATA 951 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 40, volume: 272, anno: 1997,
pagine: 25267 - 25274
SICI:
0021-9258(1997)272:40<25267:1BTISO>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
KINASE-DEPENDENT ACTIVATOR; PHOSPHATIDYLINOSITOL 3-KINASE; TRYPTOPHAN HYDROXYLASES; REGULATORY SUBUNIT; IRS-1; TYROSINE; PHOSPHORYLATION; 14-3-3-PROTEIN; DISTINCT; ASSOCIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
T. Ogihara et al., "14-3-3-PROTEIN BINDS TO INSULIN-RECEPTOR SUBSTRATE-1, ONE OF THE BINDING-SITES OF WHICH IS IN THE PHOSPHOTYROSINE BINDING DOMAIN", The Journal of biological chemistry, 272(40), 1997, pp. 25267-25274

Abstract

Insulin binding to its receptor induces the phosphorylation of cytosolic substrates, insulin receptor substrate (IRS)-1 and IRS-2, which associate with several Src homology-a domain-containing proteins. To identify unique IRS-1-binding proteins, we screened a human heart cDNA library with P-32-labeled recombinant IRS-I and obtained two isoforms (epsilon and zeta) of the 14-3-3 protein family. 14-3-3 protein has beenshown to associate with IRS-I in L6 myotubes, HepG2 hepatoma cells, Chinese hamster ovary cells, and bovine brain tissue. IRS-2, a protein structurally similar to IRS-1, was also shown to form a complex with 14-3-3 protein using a baculovirus expression system. The amount of 14-3-3 protein associated with IRS-I was not affected by insulin stimulation but was increased significantly by treatment with okadaic acid, a potent serine/threonine phosphatase inhibitor. Peptide inhibition experiments using phosphoserine-containing peptides of IFS-I revealed thatIRS-1 contains three putative binding sites for 14-3-3 protein (Ser-270, Ser-374, and Ser-641). Among these three, the motif around Ser-270is located in the phosphotyrosine binding domain of IRS-I, which is responsible for the interaction with the insulin receptor. Indeed, a truncated mutant of IRS-1 consisting of only the phosphotyrosine bindingdomain retained the capacity to bind to 14-3-3 protein in vivo. Finally, the effect of 14-3-3 protein binding on the insulin-induced phosphorylation of IRS-1 was investigated. Phosphoamino acid analysis revealed that IRS-1 coimmunoprecipitated with anti-14-3-3 antibody to be weakly phosphorylated after insulin stimulation, on tyrosine as well as serine residues, compared with IRS-l immunoprecipitated with anti-IRS-lantibody. Thus, the association with 14-3-3 protein may play a role in the regulation of insulin sensitivity by interrupting the association between the insulin receptor and IRS-1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 20:27:58