Evidence map›Paper›PMID 28147281›Full record

ArticleCell reports2017

The Atypical Ubiquitin E2 Conjugase UBE2L3 Is an Indirect Caspase-1 Target and Controls IL-1β Secretion by Inflammasomes.

Matthew J G Eldridge, Julia Sanchez-Garrido, Gil Ferreira Hoben, Philippa J Goddard, Avinash R Shenoy

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 72 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Involvement of the pyroptosis-HMGB1 axis in systemic diseases.Frontiers in cell and developmental biology · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Regulation of the Inflammasome Activation by Ubiquitination Machinery.Advances in experimental medicine and biology · 2024
    Review
  16. Review
  17. Article
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

Matthew J G EldridgeMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Julia Sanchez-GarridoMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Gil Ferreira HobenMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Philippa J GoddardMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Avinash R ShenoyMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK. Electronic address: a.shenoy@imperial.ac.uk.
Imperial College London · GB

Funding

Medical Research Council MR/J006874/1Wellcome TrustWellcome Trust 108246/Z/15/Z
6 · The paper itself

Abstract

Caspase-1 activation by inflammasome signaling scaffolds initiates inflammation and antimicrobial responses. Caspase-1 proteolytically converts newly induced pro-interleukin 1 beta (IL-1β) into its mature form and directs its secretion, triggering pyroptosis and release of non-substrate alarmins such as interleukin 1 alpha (IL-1α) and HMGB1. While some caspase-1 substrates involved in these events are known, the identities and roles of non-proteolytic targets remain unknown. Here, we use unbiased proteomics to show that the UBE2L3 ubiquitin conjugase is an indirect target of caspase-1. Caspase-1, but not caspase-4, controls pyroptosis- and ubiquitin-independent proteasomal degradation of UBE2L3 upon canonical and non-canonical inflammasome activation by sterile danger signals and bacterial infection. Mechanistically, UBE2L3 acts post-translationally to promote K48-ubiquitylation and turnover of pro-IL-1β and dampen mature-IL-1β production. UBE2L3 depletion increases pro-IL-1β levels and mature-IL-1β secretion by inflammasomes. These findings regarding UBE2L3 as a molecular rheostat have implications for IL-1-driven pathology in hereditary fever syndromes and in autoinflammatory conditions associated with UBE2L3 polymorphisms.

Indexed as

AnimalsCaspase 1InflammasomesInflammationInterleukin-1betaMiceProtein TransportProteomicsSignal TransductionUbiquitinUbiquitin-Conjugating EnzymesCaspase 1InflammasomesInterleukin-1betaUbe2l3 protein, mouseUbiquitinUbiquitin-Conjugating Enzymescaspase-1caspase-4commensalsIL-1βinflammasomesListeriaproteasomeSalmonellaUBE2L3ubiquitin

Identifiers

PMID28147281
PMCPMC5300903
OpenAlexW2585808900

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.