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Titolo:
Caspase-dependent cleavage of the hematopoietic specific adaptor protein Gads alters signalling from the T cell receptor
Autore:
Berry, DM; Benn, SJ; Cheng, AM; McGlade, CJ;
Indirizzi:
Hosp Sick Children, Arthur & Sonia Labatt Brain Tumour Res Ctr, Toronto, ON M5G 1X8, Canada Hosp Sick Children Toronto ON Canada M5G 1X8 Toronto, ON M5G 1X8, Canada Washington Univ, Sch Med, Dept Med, Div Rheumatol, St Louis, MO 63110 USA Washington Univ St Louis MO USA 63110 v Rheumatol, St Louis, MO 63110 USA
Titolo Testata:
ONCOGENE
fascicolo: 10, volume: 20, anno: 2001,
pagine: 1203 - 1211
SICI:
0950-9232(20010308)20:10<1203:CCOTHS>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOLIPASE C-GAMMA-1; TYROSINE PHOSPHOPROTEIN; MAMMALIAN CASPASES; MOLECULAR-CLONING; ACTIVATION; SLP-76; LAT; APOPTOSIS; GRB2; DEATH;
Keywords:
Gads; caspase; T cell receptor; SH2 domain; SH3 domain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: McGlade, CJ Hosp Sick Children, Arthur & Sonia Labatt Brain Tumour Res Ctr, 555 Univ Ave, Toronto, ON M5G 1X8, Canada Hosp Sick Children 555 Univ AveToronto ON Canada M5G 1X8 nada
Citazione:
D.M. Berry et al., "Caspase-dependent cleavage of the hematopoietic specific adaptor protein Gads alters signalling from the T cell receptor", ONCOGENE, 20(10), 2001, pp. 1203-1211

Abstract

Gads is a SH2 and SH3 domain-containing, hematopoietic-specific adaptor protein that functions in signalling from the T cell receptor. Gads acts by linking SLP-76, bound by the carboxy-terminal Gads SH3 domain, to tyrosine phosphorylated LAT which contains binding sites for the Gads SH2 domain. Gads is distinguished from Grb2 and the closely related Grap protein by the presence of a 120 amino acid unique region between the SH2 domain and the carboxy terminal SH3 domain. Here we demonstrate that the unique region of Gads contains a capase cleavage site. Induction of apoptosis in lymphocytes results in detectable Gads cleavage by 60 min. Gads cleavage is blocked in vivo by treating cells with a caspase 3 inhibitor. A putative caspase 3 cleavage site was identified within the unique region and mutation of this site prevented Gads cleavage in vitro, and in vivo. The Gads cleavage products retained the predicted binding specificity for SLP-76 and LAT, Expression ofthe Gads cleavage products in Jurkat T cells inhibited NFAT activation following TCR cross linking. These findings indicate that cleavage of Gads in vivo could function to alter signalling downstream of the T cell receptor by disrupting cross talk between SLP-76 and LAT.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 14:15:18