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Titolo:
DIRECT DEMONSTRATION OF AN INTRAMOLECULAR SH2-PHOSPHOTYROSINE INTERACTION IN THE CRK PROTEIN
Autore:
ROSEN MK; YAMAZAKI T; GISH GD; KAY CM; PAWSON T; KAY LE;
Indirizzi:
UNIV TORONTO,PROT ENGN NETWORK CTR EXCELLENCE,MED SCI BLDG TORONTO ONM5S 1A8 CANADA UNIV TORONTO,DEPT MED GENET TORONTO ON M5S 1A8 CANADA UNIV TORONTO,DEPT CHEM & BIOCHEM TORONTO ON M5S 1A8 CANADA MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAMME MOLEC BIOL & CANC TORONTO ON M5G 1X5 CANADA UNIV ALBERTA,DEPT BIOCHEM,MRC,PROT STRUCT & FUNCT GRP EDMONTON AB T6G2H7 CANADA
Titolo Testata:
Nature
fascicolo: 6521, volume: 374, anno: 1995,
pagine: 477 - 479
SICI:
0028-0836(1995)374:6521<477:DDOAIS>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOTYROSINE-CONTAINING PROTEINS; SH3 DOMAINS; V-CRK; BINDING; SRC; IDENTIFICATION; PRODUCT; PEPTIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
M.K. Rosen et al., "DIRECT DEMONSTRATION OF AN INTRAMOLECULAR SH2-PHOSPHOTYROSINE INTERACTION IN THE CRK PROTEIN", Nature, 374(6521), 1995, pp. 477-479

Abstract

MANY signal transduction processes are mediated by the binding Of Src-homology-2 (SH2) domains to phosphotyrosine (pTyr)-containing proteins(1). Although most SH2-pTyr interactions occur between tao different types of molecules, some appear to involve only a single molecular type. It has been proposed that the enzymatic activity and substrate recognition of the Src-family kinases(2-4), and the protein-binding and transforming activity of Crk-family adaptor proteins(5), are regulated by intramolecular SH2-pTyr interactions. In addition, the DNA-binding activity of Stat transcription factors seems to be regulated by SH2-mediated homodimerization(6). Here we examine the phosphorylated and non-phosphorylated forms of murine Crk II (p-mCrk and mCrk, respectively)(7-9) using a combination of physical techniques. The Crk protein contains a single SH2 domain and two SH3 domains in the order SH2-SH3-SH3. There is a tyrosine-phosphorylation site between the two SH3 domains at residue 221 which is phosphorylated in vivo by the Abl tyrosine kinase(5). Using NMR spectroscopic analysis, we show here that the SH2 domain of purified p-mCrk is bound to pTyr, and by hydrodynamic measurements that the phosphorylated protein is monomeric, These results provide direct demonstration of an intramolecular SH2-pTyr interaction in a signalling molecule.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:35:47