Evidence map›Paper›PMID 17502353›Full record

ArticleMolecular and cellular biology2007

Phosphorylation of Bcl10 negatively regulates T-cell receptor-mediated NF-kappaB activation.

Hu Zeng, Lie Di, Guoping Fu, Yuhong Chen, Xiang Gao, Langlai Xu, Xin Lin, Renren Wen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 37 citations in OpenAlex.

  1. A novel linker region truncating variant in BCL10 underlies a leaky immunodeficiency phenotype.Pediatric allergy and immunology : official publication of the European Society of Pediatric Allergy and Immunology · 2026
    Article
  2. Article
  3. Article
  4. Role of IκB kinase β in regulating the remodeling of the CARMA1-Bcl10-MALT1 complex.Biochemical and biophysical research communications · 2018
    Article
  5. Review
  6. Review
  7. BCL10 - Bridging CARDs to Immune Activation.Frontiers in immunology · 2018
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Regulation of NF-κB by the CARD proteins.Immunological reviews · 2012
    Review
  18. Article
  19. Review
  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

8 authors at 5 institutions in 2 countries.

Hu ZengThe Blood Research Institute, 8727 Watertown Plank Road, Milwaukee, WI 53226, USA.
Lie Di
Guoping Fu
Yuhong Chen
Xiang Gao
Langlai Xu
Xin Lin
Renren Wen
Versiti Blood Center of Wisconsin · USNanjing Agricultural University · CNModel Animal Research Center · CNNanjing University · CNThe University of Texas MD Anderson Cancer Center · US

Funding

Individual and Collaborative Roles in T Cell ActivationR01AI052327 · NIAID · BLOODCENTER OF WISCONSIN, INC. · PI WEN, RENREN · 2002 to 2005
$1.1M
NIAID NIH HHS AI52327NIAID NIH HHS R01 AI052327
6 · The paper itself

Abstract

Bcl10 (B-cell lymphoma 10) is an adaptor protein comprised of an N-terminal caspase recruitment domain and a C-terminal serine/threonine-rich domain. Bcl10 plays a critical role in antigen receptor-mediated NF-kappaB activation and lymphocyte development and functions. Our current study has discovered that T-cell activation induced monophosphorylation and biphosphorylation of Bcl10 and has identified S138 within Bcl10 as one of the T-cell receptor-induced phosphorylation sites. Alteration of S138 to an alanine residue impaired T-cell activation-induced ubiquitination and subsequent degradation of Bcl10, ultimately resulting in prolongation of TCR-mediated NF-kappaB activation and enhancement of interleukin-2 production. Taken together, our findings demonstrate that phosphorylation of Bcl10 at S138 down-regulates Bcl10 protein levels and thus negatively regulates T-cell receptor-mediated NF-kappaB activation.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsB-Cell CLL-Lymphoma 10 ProteinDown-RegulationHumansInterleukin-2Jurkat CellsLymphocyte ActivationMiceModels, BiologicalNF-kappa BPhosphorylationReceptors, Antigen, T-CellSerineUbiquitinAdaptor Proteins, Signal TransducingB-Cell CLL-Lymphoma 10 ProteinBCL10 protein, humanBcl10 protein, mouseInterleukin-2NF-kappa BReceptors, Antigen, T-CellSerineUbiquitin

Identifiers

PMID17502353
PMCPMC1951946
OpenAlexW2115245305

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.