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Thomas, Douglas D.

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751

Online
ISSN
1437-4315
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In This Section
Volume 389, Issue 10 (Oct 2008)

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Pursuing different ‘TRADDes’: TRADD signaling induced by TNF-receptor 1 and the Epstein-Barr virus oncoprotein LMP1

Arnd Kieser
  • 1Abteilung Genvektoren, Helmholtz Zentrum München – Deutsches Forschungszentrum für Gesundheit und Umwelt, Marchioninistrasse 25, D-81377 München, Germany
Published Online: 2008-08-19 | DOI: https://doi.org/10.1515/BC.2008.144

Abstract

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 TNFα, TRADD is recruited to the activated TNFR1 by direct interaction between the death domains of both molecules. TRADD mediates TNFR1 activation of NF-κB 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-κB, 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-κB 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.

Keywords: apoptosis; latent membrane protein 1 (LMP1); NF-κB; TNF-receptor 1; TRADD; transformation

About the article


Received: 2008-03-19

Accepted: 2008-06-05

Published Online: 2008-08-19

Published in Print: 2008-10-01



Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2008.144. Export Citation

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Caroline F Mohr, Martina Kalmer, Christine Gross, Melanie C Mann, Kai R Sterz, Arnd Kieser, Bernhard Fleckenstein, and Andrea K Kress
Cell Communication and Signaling, 2014, Volume 12, Number 1, Page 46
[2]
S. J. de Jong, J.-C. Albrecht, F. Giehler, A. Kieser, H. Sticht, and B. Biesinger
Science Signaling, 2013, Volume 6, Number 272, Page ra27
[3]
M Grunert, K Gottschalk, J Kapahnke, S Gündisch, A Kieser, and I Jeremias
Cell Death and Disease, 2012, Volume 3, Number 10, Page e414
[4]
L-T Wang, C-S Lin, C-Y Chai, K-Y Liu, J-Y Chen, and S-H Hsu
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Deilson Elgui de Oliveira, Gianna Ballon, and Ethel Cesarman
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[6]
Stephan Ludwig and Oliver Planz
Biological Chemistry, 2008, Volume 389, Number 10

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