Evidence map›Paper›PMID 22815893›Full record

ArticlePloS one2012

The inositol phosphatase SHIP-1 inhibits NOD2-induced NF-κB activation by disturbing the interaction of XIAP with RIP2.

Claude Condé, Xavier Rambout, Marielle Lebrun, Aurore Lecat, Emmanuel Di Valentin, Franck Dequiedt, Jacques Piette, Geoffrey Gloire, Sylvie Legrand

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Trial
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  7. Article
  8. Article
  9. Review
  10. Genes · 2023
    Review
  11. Review
  12. RIP2 promotes FcγR-mediated reactive oxygen species production.The Journal of biological chemistry · 2019
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
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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

9 authors at 1 institution in 1 country.

Claude CondéLaboratory of Virology and Immunology, Signal Transduction Unit, GIGA-R, University of Liège, Liège, Belgium.
Xavier Rambout
Marielle Lebrun
Aurore Lecat
Emmanuel Di Valentin
Franck Dequiedt
Jacques Piette
Geoffrey Gloire
Sylvie Legrand
University of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SHIP-1 is an inositol phosphatase predominantly expressed in hematopoietic cells. Over the ten past years, SHIP-1 has been described as an important regulator of immune functions. Here, we characterize a new inhibitory function for SHIP-1 in NOD2 signaling. NOD2 is a crucial cytoplasmic bacterial sensor that activates proinflammatory and antimicrobial responses upon bacterial invasion. We observed that SHIP-1 decreases NOD2-induced NF-κB activation in macrophages. This negative regulation relies on its interaction with XIAP. Indeed, we observed that XIAP is an essential mediator of the NOD2 signaling pathway that enables proper NF-κB activation in macrophages. Upon NOD2 activation, SHIP-1 C-terminal proline rich domain (PRD) interacts with XIAP, thereby disturbing the interaction between XIAP and RIP2 in order to decrease NF-κB signaling.

Indexed as

Cell Line, TumorDown-RegulationEpithelial CellsGene Expression RegulationHumansImmune SystemInflammationInositol Polyphosphate 5-PhosphatasesMacrophagesModels, BiologicalMonocytesNF-kappa BNod2 Signaling Adaptor ProteinPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoric Monoester HydrolasesProtein Structure, TertiaryInositol Polyphosphate 5-PhosphatasesINPP5D protein, humanNF-kappa BNOD2 protein, humanNod2 Signaling Adaptor ProteinPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoric Monoester HydrolasesReceptor-Interacting Protein Serine-Threonine Kinase 2RIPK2 protein, humanXIAP protein, humanX-Linked Inhibitor of Apoptosis Protein

Identifiers

PMID22815893
PMCPMC3398883
OpenAlexW2022192437

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.