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Titolo:
TUMOR-NECROSIS-FACTOR RECEPTOR-ASSOCIATED FACTOR-2 IS A MEDIATOR OF NF-KAPPA-B ACTIVATION BY LATENT INFECTION MEMBRANE-PROTEIN-1, THE EPSTEIN-BARR-VIRUS TRANSFORMING PROTEIN
Autore:
KAYE KM; DEVERGNE O; HARADA JN; IZUMI KM; YALAMANCHILI R; KIEFF E; MOSIALOS G;
Indirizzi:
HARVARD UNIV,BRIGHAM & WOMENS HOSP,SCH MED,DEPT MED,75 FRANCIS ST BOSTON MA 02115 HARVARD UNIV,BRIGHAM & WOMENS HOSP,SCH MED,DEPT MICROBIOL & MOL GENETBOSTON MA 02115
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 20, volume: 93, anno: 1996,
pagine: 11085 - 11090
SICI:
0027-8424(1996)93:20<11085:TRFIAM>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
LYMPHOCYTE GROWTH TRANSFORMATION; TERMINAL CYTOPLASMIC DOMAIN; RING FINGER PROTEIN; BNLF-1 ONCOGENE; LMP1; CELLS; CD40; EXPRESSION; INDUCTION; FAMILY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
K.M. Kaye et al., "TUMOR-NECROSIS-FACTOR RECEPTOR-ASSOCIATED FACTOR-2 IS A MEDIATOR OF NF-KAPPA-B ACTIVATION BY LATENT INFECTION MEMBRANE-PROTEIN-1, THE EPSTEIN-BARR-VIRUS TRANSFORMING PROTEIN", Proceedings of the National Academy of Sciences of the United Statesof America, 93(20), 1996, pp. 11085-11090

Abstract

Latent infection membrane protein 1 (LMP1), the Epstein-Barr virus transforming protein, associates with tumor necrosis factor receptor (TNFR) associated factor 1 (TRAF1) and TRAF3, Since TRAF2 has been implicated in TNFR-mediated NF-kappa B activation, we have evaluated the role of TRAF2 in LMP1-mediated NF-kappa B activation, TRAF2 binds in vitro to the LMP1 carboxyl-terminal cytoplasmic domain (CT), coprecipitates with LMP1 in B lymphoblasts, and relocalizes to LMP1 plasma membranepatches. A dominant negative TRAF2 deletion mutant that lacks amino acids 6-86 (TRAF2 Delta 6-86) inhibits NF-KB activation from the LMP1 CT and competes with TRAF2 for LMP1 binding, TRAF2 Delta 6-86 inhibits NF-kappa B activation mediated by the first 45 amino acids of the LMP1CT by more than 75% but inhibits NF-kappa B activation through the last 55 amino acids of the CT by less than 40%. A TRAF interacting protein, TANK, inhibits NF-kappa B activation by more than 70% from both LMP1 CT domains. These data implicate TRAF2 aggregation in NF-kappa B activation by the first 45 amino acids of the LMP1 CT and suggest that adifferent TRAF-related pathway may be involved in NF-kappa B activation by the last 55 amino acids of the LMP1 CT.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 00:59:24