Evidence map›Paper›PMID 32614325›Full record

ArticleeLife2020

Interaction mapping of endoplasmic reticulum ubiquitin ligases identifies modulators of innate immune signalling.

Emma J Fenech, Federica Lari, Philip D Charles, Roman Fischer, Marie Laétitia-Thézénas, Katrin Bagola, Adrienne W Paton, James C Paton, Mads Gyrd-Hansen, Benedikt M Kessler and 1 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

58 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
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  8. Article
  9. Article
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  11. Article
  12. Article
  13. Article
  14. Article
  15. O-GlcNAc of STING mediates antiviral innate immunity.Cell communication and signaling : CCS · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Unravelling turbot (Frontiers in immunology · 2024
    Article
  20. Review
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

11 authors at 4 institutions in 3 countries.

Emma J FenechLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom.ORCID 0000-0003-4414-3233
Federica LariLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom.
Philip D CharlesTDI Mass Spectrometry Laboratory, Target Discovery Institute, University of Oxford, Oxford, United Kingdom.ORCID 0000-0001-5278-5354
Roman FischerTDI Mass Spectrometry Laboratory, Target Discovery Institute, University of Oxford, Oxford, United Kingdom.ORCID 0000-0002-9715-5951
Marie Laétitia-ThézénasTDI Mass Spectrometry Laboratory, Target Discovery Institute, University of Oxford, Oxford, United Kingdom.
Katrin BagolaLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom.
Adrienne W PatonResearch Centre for Infectious Diseases, Department of Molecular and Biomedical Science, University of Adelaide, Adelaide, Australia.
James C PatonResearch Centre for Infectious Diseases, Department of Molecular and Biomedical Science, University of Adelaide, Adelaide, Australia.
Mads Gyrd-HansenLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom.ORCID 0000-0001-5641-5019
Benedikt M KesslerTDI Mass Spectrometry Laboratory, Target Discovery Institute, University of Oxford, Oxford, United Kingdom.ORCID 0000-0002-8160-2446
John C ChristiansonLudwig Institute for Cancer Research, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom.ORCID 0000-0002-0474-1207
University of Oxford · GBThe University of Adelaide · AUAcademy of Medical Sciences · GBNuffield Orthopaedic Centre · GB

Funding

Cancer Research UK 29217Medical Research Council MR/L001209/1Wellcome Trust
6 · The paper itself

Abstract

Ubiquitin ligases (E3s) embedded in the endoplasmic reticulum (ER) membrane regulate essential cellular activities including protein quality control, calcium flux, and sterol homeostasis. At least 25 different, transmembrane domain (TMD)-containing E3s are predicted to be ER-localised, but for most their organisation and cellular roles remain poorly defined. Using a comparative proteomic workflow, we mapped over 450 protein-protein interactions for 21 stably expressed, full-length E3s. Bioinformatic analysis linked ER-E3s and their interactors to multiple homeostatic, regulatory, and metabolic pathways. Among these were four membrane-embedded interactors of RNF26, a polytopic E3 whose abundance is auto-regulated by ubiquitin-proteasome dependent degradation. RNF26 co-assembles with TMEM43, ENDOD1, TMEM33 and TMED1 to form a complex capable of modulating innate immune signalling through the cGAS-STING pathway. This RNF26 complex represents a new modulatory axis of STING and innate immune signalling at the ER membrane. Collectively, these data reveal the broad scope of regulation and differential functionalities mediated by ER-E3s for both membrane-tethered and cytoplasmic processes.

Indexed as

Immunity, InnateProtein Interaction MappingProtein Interaction MapsSignal TransductionEndoplasmic ReticulumProteomicsUbiquitin-Protein LigasesUbiquitin-Protein Ligasescell biologyendoplasmic reticulumimmunologyinflammationinnate immune responsenoneRNF26STINGubiquitin ligase

Identifiers

PMID32614325
PMCPMC7332293
OpenAlexW3034852029

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.