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Titolo:
THE PROTEIN PRODUCT OF THE C-CBL PROTOONCOGENE IS THE 120-KDA TYROSINE-PHOSPHORYLATED PROTEIN IN JURKAT CELLS ACTIVATED VIA THE T-CELL ANTIGEN RECEPTOR
Autore:
DONOVAN JA; WANGE RL; LANGDON WY; SAMELSON LE;
Indirizzi:
NICHHD,CELL BIOL & METAB BRANCH BETHESDA MD 20892 NICHHD,CELL BIOL & METAB BRANCH BETHESDA MD 20892 UNIV WESTERN AUSTRALIA,DEPT BIOCHEM NEDLANDS WA 6009 AUSTRALIA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 37, volume: 269, anno: 1994,
pagine: 22921 - 22924
SICI:
0021-9258(1994)269:37<22921:TPPOTC>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
ZETA-CHAIN; SIGNAL TRANSDUCTION; LYMPHOCYTES-T; V-CBL; KINASE; SH2; ASSOCIATION; ONCOGENE; BINDING; ZAP-70;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
J.A. Donovan et al., "THE PROTEIN PRODUCT OF THE C-CBL PROTOONCOGENE IS THE 120-KDA TYROSINE-PHOSPHORYLATED PROTEIN IN JURKAT CELLS ACTIVATED VIA THE T-CELL ANTIGEN RECEPTOR", The Journal of biological chemistry, 269(37), 1994, pp. 22921-22924

Abstract

Tyrosine phosphorylation of multiple cellular proteins is a critical event in T cell receptor (TCR)-mediated activation. This pathway has also been implicated in cellular transformation in multiple systems. The viral oncogene v-cbl is the transforming gene of a murine retrovirusthat induces pre-B cell lymphomas and myelogenous leukemias. The product of its cellular homolog, p120(cbl), is a 120-kDa cytoplasmic protein that is nontransforming when overexpressed. Here we show that the 120-kDa protein tyrosine phosphorylated in Jurkat T cells upon TCR engagement is p120(cbl). Following stimulation through the TCR, this tyrosine phosphorylation is rapid and reversible. Tyrosine-phosphorylated p120(cbl) binds to glutathione S-transferase fusion proteins generated from SH2 domains of the Fyn, Lck, and Blk protein tyrosine kinases, GTPase-activating protein and phospholipase Cy. The p120(cbl) from unactivated and activated cells also binds to full-length glutathione S-transferase-Grb2 and the Grb2 N-terminal SH3 domain, but not to the Grb2 C-terminal SH3 domain. Additionally, p120(cbl) binds to SH3 domains ofFyn and Lck, but not Blk. These data expand our knowledge of protein tyro sine kinase signaling pathways in T cells by identifying a prominent tyrosine kinase substrate. This protein, the product of the cellular homolog of a transforming oncogene, can interact with several knownsignaling molecules.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 20:04:02