Evidence map›Paper›PMID 14576817›Full record

ArticleOncogene2003

Epstein-Barr virus-encoded latent infection membrane protein 1 regulates the processing of p100 NF-kappaB2 to p52 via an IKKgamma/NEMO-independent signalling pathway.

Aristides G Eliopoulos, Jorge H Caamano, Joanne Flavell, Gary M Reynolds, Paul G Murray, Jean-Luc Poyet, Lawrence S Young

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Development of RelB-targeting small-molecule inhibitors of non-canonical NF-κB signaling with antitumor efficacy.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
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  9. Advances in targeted therapy for malignant lymphoma.Signal transduction and targeted therapy · 2020
    Review
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  12. Review
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  14. Review
  15. Phosphorylation: Implications in Cancer.The protein journal · 2017
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Aristides G EliopoulosCancer Research UK Institute for Cancer Studies, The University of Birmingham Medical School, Birmingham B15 2TA, UK. A.G.Eliopoulos@bham.ac.uk
Jorge H Caamano
Joanne Flavell
Gary M Reynolds
Paul G Murray
Jean-Luc Poyet
Lawrence S Young
Cancer Research UK · GBImmune Regulation (United Kingdom) · GBInserm · FRUniversity of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The oncogenic Epstein-Barr virus (EBV)-encoded latent infection membrane protein 1 (LMP1) constitutively activates the 'canonical' NF-kappaB pathway that involves the phosphorylation and degradation of IkappaBalpha downstream of the IkappaB kinases (IKKs). In this study, we show that LMP1 also promotes the proteasome-mediated proteolysis of p100 NF-kappaB2 resulting in the generation of active p52, which translocates to the nucleus in complex with the p65 and RelB NF-kappaB subunits. LMP1-induced NF-kappaB transactivation is reduced in nf-kb2(-/-) mouse embryo fibroblasts, suggesting that p100 processing contributes to LMP1-mediated NF-kappaB transcriptional effects. This pathway is likely to operate in vivo, as the expression of LMP1 in primary EBV-positive Hodgkin's lymphoma and nasopharyngeal carcinoma biopsies correlates with the nuclear accumulation of p52. Interestingly, while the ability of LMP1 to activate the canonical NF-kappaB pathway is impaired in cells lacking IKKgamma/NEMO, the regulatory subunit of the IKK complex, p100 processing remains unaffected. As a result, nuclear translocation of p52, but not p65, occurs in the absence of IKKgamma. These data point to the existence of a novel signalling pathway that regulates NF-kappaB in LMP1-expressing cells, and may thereby play a role in both oncogenic transformation and the establishment of persistent EBV infection.

Indexed as

Signal TransductionActive Transport, Cell NucleusAnimalsCell Line, TumorElectrophoretic Mobility Shift AssayHumansI-kappa B KinaseMiceNF-kappa BNF-kappa B p52 SubunitProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesTranscriptional ActivationTranscription Factor RelATransfectionViral Matrix ProteinsCHUK protein, humanChuk protein, mouseEBV-associated membrane antigen, Epstein-Barr virusI-kappa B KinaseIKBKB protein, humanIkbkb protein, mouseIKBKE protein, humanIkbke protein, mouseNF-kappa BNF-kappa B p52 SubunitProtein Serine-Threonine KinasesTranscription Factor RelAViral Matrix Proteins

Identifiers

PMID14576817
OpenAlexW1500780819

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.