Evidence map›Paper›PMID 16446357›Full record

ArticleThe Journal of biological chemistry2006

TAK1 is a component of the Epstein-Barr virus LMP1 complex and is essential for activation of JNK but not of NF-kappaB.

Noriyuki Uemura, Taisuke Kajino, Hideki Sanjo, Shintaro Sato, Shizuo Akira, Kunihiro Matsumoto, Jun Ninomiya-Tsuji

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 41 citations in OpenAlex.

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  9. The interaction between mitochondria and oncoviruses.Biochimica et biophysica acta. Molecular basis of disease · 2018
    Review
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  19. TRAF5 is a critical mediator of in vitro signals and in vivo functions of LMP1, the viral oncogenic mimic of CD40.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 5 institutions in 2 countries.

Noriyuki UemuraDepartment of Molecular Biology, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
Taisuke Kajino
Hideki Sanjo
Shintaro Sato
Shizuo Akira
Kunihiro Matsumoto
Jun Ninomiya-Tsuji
Nagoya University · JPOsaka University · JPJapan Science and Technology Agency · JPNorth Carolina State University · USRIKEN Center for Integrative Medical Sciences · JP

Funding

TAK1 signaling network in tissue homeostasisR01GM068812 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI NINOMIYA-TSUJI, JUN · 2004 to 2013
$2.4M
ROLE OF TAK1 IN RANKL SIGNALING PATHWAYR21AR050972 · NIAMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI NINOMIYA-TSUJI, JUN · 2004 to 2005
$286k
NIAMS NIH HHS AR050972NIAMS NIH HHS R21 AR050972NIGMS NIH HHS GM068812NIGMS NIH HHS R01 GM068812
6 · The paper itself

Abstract

Epstein-Barr virus latent membrane protein 1 (LMP1) activates NF-kappaB and c-Jun N-terminal kinase (JNK), which is essential for LMP1 oncogenic activity. Genetic analysis has revealed that tumor necrosis factor receptor-associated factor 6 (TRAF6) is an indispensable intermediate of LMP1 signaling leading to activation of both NF-kappaB and JNK. However, the mechanism by which LMP1 engages TRAF6 for activation of NF-kappaB and JNK is not well understood. Here we demonstrate that TAK1 mitogen-activated protein kinase kinase kinase and TAK1-binding protein 2 (TAB2), together with TRAF6, are recruited to LMP1 through its N-terminal transmembrane region. The C-terminal cytoplasmic region of LMP1 facilitates the assembly of this complex and enhances activation of JNK. In contrast, IkappaB kinase gamma is recruited through the C-terminal cytoplasmic region and this is essential for activation of NF-kappaB. Furthermore, we found that ablation of TAK1 resulted in the loss of LMP1-induced activation of JNK but not of NF-kappaB. These results suggest that an LMP1-associated complex containing TRAF6, TAB2, and TAK1 plays an essential role in the activation of JNK. However, TAK1 is not an exclusive intermediate for NF-kappaB activation in LMP1 signaling.

Indexed as

AnimalsCell LineCytoplasmEnzyme ActivationEnzyme InhibitorsFibroblastsGene DeletionHerpesvirus 4, HumanHumansImmunoblottingMAP Kinase Kinase 4MAP Kinase Kinase Kinase 7MAP Kinase Kinase KinasesMiceMice, TransgenicModels, BiologicalEBV-associated membrane antigen, Epstein-Barr virusEnzyme InhibitorsMAP Kinase Kinase 4MAP Kinase Kinase Kinase 7MAP Kinase Kinase KinasesNF-kappa BTNF Receptor-Associated Factor 6Viral Matrix Proteins

Identifiers

PMID16446357
PMCPMC1797069
OpenAlexW1991902573

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.