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Open Access Gold möglich sobald Verlagsversion bei der ZB eingereicht worden ist.
Pursuing different 'TRADDes': TRADD signaling induced by TNF-receptor 1 and the Epstein-Barr virus oncoprotein LMP1.
Biol. Chem. 389, 1261-1271 (2008)
The pro-apoptotic tumor necrosis factor (TNF)-receptor 1-associated death domain protein (TRADD) was initially identified as the central signaling adapter molecule of TNF-receptor 1 (TNFR1). Upon stimulation with the pro-inflammatory cytokine TNFalpha, TRADD is recruited to the activated TNFR1 by direct interaction between the death domains of both molecules. TRADD mediates TNFR1 activation of NF-kappaB and c-Jun N-terminal kinase (JNK), as well as caspase-dependent apoptosis. Surprisingly, TRADD is also recruited by latent membrane protein 1 (LMP1), the major oncoprotein of the human Epstein-Barr tumor virus. By mimicking a constitutively active receptor, LMP1 is essential for B-cell transformation by the virus, activating NF-kappaB, phosphatidylinositol 3-kinase, JAK/STAT and mitogen-activated protein kinase signaling. In contrast to TNFR1, LMP1's interaction with TRADD is independent of a functional death domain. The unique structure of the LMP1-TRADD complex dictates an unusual type of TRADD-dependent NF-kappaB signaling and subverts TRADD's potential to induce apoptosis. This article provides an overview of TNFR1 and LMP1 signal transduction with a focus on TRADD's functions in apoptotic and transforming signaling, incorporating recent results from TRADD RNAi and knockout studies.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Times Cited
Altmetric
2.840
0.780
54
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern
Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
apoptosis; latent membrane protein 1 (LMP1); NF-kB; TNF-receptor 1; TRADD; transformation
Sprache
englisch
Veröffentlichungsjahr
2008
HGF-Berichtsjahr
0
ISSN (print) / ISBN
1431-6730
e-ISSN
1437-4315
Zeitschrift
Biological Chemistry
Quellenangaben
Band: 389,
Heft: 10,
Seiten: 1261-1271
Verlag
de Gruyter
Begutachtungsstatus
Peer reviewed
Institut(e)
Research Unit Gene Vector (AGV)
POF Topic(s)
30203 - Molecular Targets and Therapies
Forschungsfeld(er)
Immune Response and Infection
PSP-Element(e)
G-501500-001
DOI
10.1515/BC.2008
Erfassungsdatum
2008-12-15