Evidence map›Paper›PMID 38536929›Full record

ArticleScience advances2024

Discovery and characterization of noncanonical E2-conjugating enzymes.

Syed Arif Abdul Rehman, Chiara Cazzaniga, Elena Di Nisio, Odetta Antico, Axel Knebel, Clare Johnson, Alp T Şahin, Peter E G F Ibrahim, Frederic Lamoliatte, Rodolfo Negri and 2 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. UBE2L6 drives ulcerative colitis progression by promoting BIRC2 degradation and activating non-canonical NF-κB signalling.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Tracking E2-specific substrates.Nature chemical biology · 2025
    Article
  8. Article
  9. Insights into non-proteinaceous ubiquitination.Biochemical Society transactions · 2025
    Review
  10. Article
  11. Article
  12. Review
  13. Editorial: Reviews in ubiquitin signaling: 2022.Frontiers in molecular biosciences · 2023
    Article
  14. 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 3 institutions in 3 countries.

Syed Arif Abdul RehmanMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.ORCID 0000-0002-8652-4491
Chiara CazzanigaMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.ORCID 0000-0002-7693-9167
Elena Di NisioMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.ORCID 0000-0001-7295-3941
Odetta AnticoMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.ORCID 0000-0002-7325-3303
Axel KnebelMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.
Clare JohnsonMRCPPU Reagents and Services, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.
Alp T ŞahinComputational Biology, School of Life Sciences, University of Dundee, Dundee, UK.ORCID 0000-0002-0829-7940
Peter E G F IbrahimDrug Discovery Unit, Division of Biological Chemistry and Drug Discovery, University of Dundee, Dow St, Dundee DD1 5EH, UK.
Frederic LamoliatteMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.
Rodolfo NegriDepartment of Biology and Biotechnologies "C. Darwin", Sapienza University of Rome, via dei Sardi, 70 00185 Rome, Italy.ORCID 0000-0002-4806-7090
Miratul M K MuqitMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.ORCID 0000-0001-9733-2404
Virginia De CesareMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.ORCID 0000-0002-2640-6389
MRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GBInstitute of Molecular Biology and Pathology · IT

Funding

Medical Research Council MR/V025759/1
6 · The paper itself

Abstract

E2-conjugating enzymes (E2s) play a central role in the enzymatic cascade that leads to the attachment of ubiquitin to a substrate. This process, termed ubiquitylation, is required to maintain cellular homeostasis and affects almost all cellular process. By interacting with multiple E3 ligases, E2s dictate the ubiquitylation landscape within the cell. Since its discovery, ubiquitylation has been regarded as a posttranslational modification that specifically targets lysine side chains (canonical ubiquitylation). We used Matrix-Assisted Laser Desorption/Ionization-Time Of Flight Mass Spectrometry to identify and characterize a family of E2s that are instead able to conjugate ubiquitin to serine and/or threonine. We used structural modeling and prediction tools to identify the key activity determinants that these E2s use to interact with ubiquitin as well as their substrates. Our results unveil the missing E2s necessary for noncanonical ubiquitylation, underscoring the adaptability and versatility of ubiquitin modifications.

Indexed as

Ubiquitin-Conjugating EnzymesUbiquitin-Protein LigasesProtein Processing, Post-TranslationalUbiquitinUbiquitinationUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID38536929
PMCPMC10971424
OpenAlexW4393246004

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.