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http://purl.uniprot.org/citations/8855313http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8855313http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8855313http://www.w3.org/2000/01/rdf-schema#comment"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 membrane patches. A dominant negative TRAF2 deletion mutant that lacks amino acids 6-86 (TRAF/ delta 6-86) inhibits NF-kappa B 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 LMP1 CT 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 a different TRAF-related pathway may be involved in NF-kappa B activation by the last 55 amino acids of the LMP1 CT."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.org/dc/terms/identifier"doi:10.1073/pnas.93.20.11085"xsd:string
http://purl.uniprot.org/citations/8855313http://purl.org/dc/terms/identifier"doi:10.1073/pnas.93.20.11085"xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Kieff E."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Kieff E."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Izumi K.M."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Izumi K.M."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Kaye K.M."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Kaye K.M."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Mosialos G."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Mosialos G."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Devergne O."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Devergne O."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Harada J.N."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Harada J.N."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Yalamanchili R."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/author"Yalamanchili R."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/pages"11085-11090"xsd:string
http://purl.uniprot.org/citations/8855313http://purl.uniprot.org/core/pages"11085-11090"xsd:string