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Titolo:
REGULATION OF THE ASSOCIATION OF P120(CBL) WITH GRB2 IN JURKAT T-CELLS
Autore:
DONOVAN JA; OTA Y; LANGDON WY; SAMELSON LE;
Indirizzi:
NICHHD,CELL BIOL & METAB BRANCH,NIH,BLDG 18T,RM 101 BETHESDA MD 20892 NICHHD,CELL BIOL & METAB BRANCH,NIH BETHESDA MD 20892 UNIV WESTERN AUSTRALIA NEDLANDS WA 6009 AUSTRALIA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 42, volume: 271, anno: 1996,
pagine: 26369 - 26374
SICI:
0021-9258(1996)271:42<26369:ROTAOP>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; C-CBL PROTOONCOGENE; RECEPTOR SIGNAL TRANSDUCTION; ANTIGEN RECEPTOR; SH3 DOMAIN; ZETA-CHAIN; PHOSPHORYLATED PROTEIN; HEMATOPOIETIC-CELLS; EXCHANGE PROTEIN; V-CBL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
59
Recensione:
Indirizzi per estratti:
Citazione:
J.A. Donovan et al., "REGULATION OF THE ASSOCIATION OF P120(CBL) WITH GRB2 IN JURKAT T-CELLS", The Journal of biological chemistry, 271(42), 1996, pp. 26369-26374

Abstract

The c-cbl protooncogene product (p120(cbl)) is a known substrate of multiple tyrosine kinases. It is found in complexes with critical signal transduction molecules, including the linker protein Grb2. Here, we demonstrate using an immobilized Grb2-binding peptide that the Grb2-p120(cbl) complex dissociates in vivo following engagement of the T-cellantigen receptor in Jurkat T-cells. The early kinetics of this dissociation correlate with the known time course of tyrosine phosphorylation of p120(cbl) and other substrates. This dissociation persists In vivo even when p120(cbl) becomes dephosphorylated to basal levels. However, this decreased association is not observed in protein overlay assays on nitrocellulose membranes in which a Grb2 fusion protein is used to detect p120(cbl) from stimulated or unstimulated cells. These data suggest that the tyrosine phosphorylation of p120(cbl) does not completely account for the regulation of its association with Grb2. Additionally, we used truncation mutations of p120(cbl) to map the p120(cbl)-Grb2 interaction to amino acids 481-528 of p120(cbl); this interaction is stronger in longer constructs that include additional proline-rich motifs. The in vivo regulation of the Grb2-p120(cbl) complex further supports the idea of a significant role for p120(cbl) in receptor-mediated signaling pathways.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 19:53:38