Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
ASSOCIATION OF P62, A MULTIFUNCTIONAL SH2-DOMAIN AND SH3-DOMAIN BINDING-PROTEIN, WITH SRC FAMILY TYROSINE KINASES, GRB2, AND PHOSPHOLIPASE-C-GAMMA-1
Autore:
RICHARD S; YU DY; BLUMER KJ; HAUSLADEN D; OLSZOWY MW; CONNELLY PA; SHAW AS;
Indirizzi:
ST LOUIS UNIV,SCH MED,CTR IMMUNOL,BOX 8118 ST LOUIS MO 63110 ST LOUIS UNIV,SCH MED,CTR IMMUNOL ST LOUIS MO 63110 ST LOUIS UNIV,SCH MED,DEPT PATHOL ST LOUIS MO 63110 ST LOUIS UNIV,SCH MED,DEPT PHYSIOL & CELL BIOL ST LOUIS MO 63110 PFIZER INC,DIV CENT RES GROTON CT 06340
Titolo Testata:
Molecular and cellular biology
fascicolo: 1, volume: 15, anno: 1995,
pagine: 186 - 197
SICI:
0270-7306(1995)15:1<186:AOPAMS>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEIN; GAP-ASSOCIATED PROTEINS; AMINO-TERMINAL DOMAIN; RNA-BINDING PROTEINS; C-SRC; SIGNAL TRANSDUCTION; T-CELL; PHOSPHATIDYLINOSITOL 3'-KINASE; PHOSPHORYLATED PEPTIDES; TRANSFORMING PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
88
Recensione:
Indirizzi per estratti:
Citazione:
S. Richard et al., "ASSOCIATION OF P62, A MULTIFUNCTIONAL SH2-DOMAIN AND SH3-DOMAIN BINDING-PROTEIN, WITH SRC FAMILY TYROSINE KINASES, GRB2, AND PHOSPHOLIPASE-C-GAMMA-1", Molecular and cellular biology, 15(1), 1995, pp. 186-197

Abstract

src family tyrosine kinases contain two noncatalytic domains termed src homology 3 (SH3) and SH2 domains. Although several other signal transduction molecules also contain tandemly occurring SH3 and SH2 domains, the function of these closely spaced domains is not well understood. To identify the role of the SH3 domains of src family tyrosine kinases, we sought to identify proteins that interacted with this domain. By using the yeast two-hybrid system, we identified p62, a tyrosine-phosphorylated protein that associates with p21(ras) GTPase-activating protein, as a src family kinase SH3-domain-binding protein. Reconstitution of complexes containing p62 and the src family kinase p59(fyn) in HeLa cells demonstrated that complex formation resulted in tyrosine phosphorylation of p62 and was mediated by both the SH3 and SH2 domains of p59(fyn). The phosphorylation of p62 by p59(fyn) required an intact SH3 domain, demonstrating that one function of the src family kinase SH3 domains is to bind and present certain substrates to the kinase. Asp62 contains at least five SH3 domain-binding motifs and multiple tyrosine phosphorylation sites, p62 may interact with other signalling molecules via SH3 and SH2 domain interactions. Here we show that the SH3and/or SH2 domains of the signalling proteins Grb2 and phospholipase C gamma-1 can interact with p62 both in vitro and in vivo. Thus, we propose that one function of the tandemly occurring SH3 and SH2 domains of src family kinases is to bind p62, a multifunctional SH3 and SH2 domain adapter protein, linking src family kinases to downstream effector and regulatory molecules.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 10:28:45