Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
BIOCHEMICAL AND GENETIC-ANALYSIS OF THE DRK SH2 SH3 ADAPTER PROTEIN OF DROSOPHILA/
Autore:
RAABE T; OLIVIER JP; DICKSON B; LIU XD; GISH GD; PAWSON T; HAFEN E;
Indirizzi:
UNIV WURZBURG,THEODOR BOVERI INST,LEHRSTUHL GENET D-97074 WURZBURG GERMANY MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAMME MOLEC BIOL & CANC TORONTO ON M5G 1X5 CANADA UNIV ZURICH,INST ZOOL CH-8057 ZURICH SWITZERLAND
Titolo Testata:
EMBO journal
fascicolo: 11, volume: 14, anno: 1995,
pagine: 2509 - 2518
SICI:
0261-4189(1995)14:11<2509:BAGOTD>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR TYROSINE KINASES; SH3 DOMAINS; SIGNAL-TRANSDUCTION; PHOSPHOTYROSINE PHOSPHATASE; NUCLEOTIDE EXCHANGE; SEVENLESS PROTEIN; INSULIN-RECEPTOR; MITOGENIC SIGNAL; GRB2; ACTIVATION;
Keywords:
DROSOPHILA; SEVENLESS; SIGNAL TRANSDUCTION; SOS; SH2 ADAPTER PROTEIN; SH3 DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
T. Raabe et al., "BIOCHEMICAL AND GENETIC-ANALYSIS OF THE DRK SH2 SH3 ADAPTER PROTEIN OF DROSOPHILA/", EMBO journal, 14(11), 1995, pp. 2509-2518

Abstract

The Drk SH3-SH2-SH3 adaptor protein has been genetically identified in a screen for rate-limiting components acting downstream of the Sevenless (Sev) receptor tyrosine kinase in the developing eye of Drosophila, It provides a link between the activated Sev receptor and Sos, a guanine nucleotide release factor that activates Ras1. We have used a combined biochemical and genetic approach to study the interactions between Sev, Drk and Sos. We show that Tyr2546 in the cytoplasmic tail of Sev is required for Drk binding, probably because it provides a recognition site for the Drk SH2 domain. Interestingly, a mutation at this site does not completely block Sev function in vivo. This may suggest that Sev can signal in a Drk-independent, parallel pathway or that Drk can also bind to an intermediate docking protein. Analysis of the Drk-Sos interaction has identified a high affinity binding site for Drk SH3 domains in the Sos tail. We show that the N-terminal Drk SH3 domain is primarily responsible for binding to the tail of Sos in vitro, and for signalling to Ras in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 12:26:19