Evidence map›Paper›PMID 22700971›Full record

ArticleThe Journal of biological chemistry2012

The c-Jun N-terminal kinase (JNK)-binding protein (JNKBP1) acts as a negative regulator of NOD2 protein signaling by inhibiting its oligomerization process.

Aurore Lecat, Emmanuel Di Valentin, Joan Somja, Samuel Jourdan, Marianne Fillet, Thomas A Kufer, Yvette Habraken, Catherine Sadzot, Edouard Louis, Philippe Delvenne and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Resolving the field: a role for Nod2 in T cells.Journal of immunology (Baltimore, Md. : 1950) · 2025
    Review
  2. Article
  3. Article
  4. Novel pathogenicClinical kidney journal · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. NOD2 and inflammation: current insights.Journal of inflammation research · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. 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

12 authors at 2 institutions in 5 countries.

Aurore LecatLaboratory of Virology and Immunology, GIGA-R, B34, University of Liege, B-4000 Liege, Belgium.
Emmanuel Di Valentin
Joan Somja
Samuel Jourdan
Marianne Fillet
Thomas A Kufer
Yvette Habraken
Catherine Sadzot
Edouard Louis
Philippe Delvenne
Jacques Piette
Sylvie Legrand-Poels
University of Liège · BEUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NOD2 is one of the best characterized members of the cytosolic NOD-like receptor family. NOD2 is able to sense muramyl dipeptide, a specific bacterial cell wall component, and to subsequently induce various signaling pathways leading to NF-κB activation and autophagy, both events contributing to an efficient innate and adaptive immune response. Interestingly, loss-of-function NOD2 variants were associated with a higher susceptibility for Crohn disease, which highlights the physiological importance of proper regulation of NOD2 activity. We performed a biochemical screen to search for new NOD2 regulators. We identified a new NOD2 partner, c-Jun N-terminal kinase-binding protein 1 (JNKBP1), a scaffold protein characterized by an N-terminal WD-40 domain. JNKBP1, through its WD-40 domain, binds to NOD2 following muramyl dipeptide activation. This interaction attenuates NOD2-mediated NF-κB activation and IL-8 secretion as well as NOD2 antibacterial activity. JNKBP1 exerts its repressor effect by disturbing NOD2 oligomerization and RIP2 tyrosine phosphorylation, both steps required for downstream NOD2 signaling. We furthermore showed that JNKBP1 and NOD2 are co-expressed in the human intestinal epithelium and in immune cells recruited in the lamina propria, which suggests that JNKBP1 contributes to maintain NOD2-mediated intestinal immune homeostasis.

Indexed as

HEK293 CellsHumansInterleukin-8Intestinal MucosaIntracellular Signaling Peptides and ProteinsJurkat CellsNF-kappa BNod2 Signaling Adaptor ProteinPhosphorylationProtein MultimerizationProtein Structure, TertiaryReceptor-Interacting Protein Serine-Threonine Kinase 2Signal TransductionU937 CellsCXCL8 protein, humanInterleukin-8Intracellular Signaling Peptides and ProteinsNF-kappa BNOD2 protein, humanNod2 Signaling Adaptor ProteinReceptor-Interacting Protein Serine-Threonine Kinase 2RIPK2 protein, human

Identifiers

PMID22700971
PMCPMC3436148
OpenAlexW2044789038

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.