Evidence map›Paper›PMID 24076655›Full record

ArticleThe EMBO journal2013

TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes.

Ian R Kelsall, David M Duda, Jennifer L Olszewski, Kay Hofmann, Axel Knebel, Frédéric Langevin, Nicola Wood, Melanie Wightman, Brenda A Schulman, Arno F Alpi

Abstract read
In one paragraph

Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
–field-weighted citation impact
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

74 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. E2 variants for probing E3 ubiquitin ligase activities.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  9. Article
  10. Cul5bioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Biochemical analysis of PD-L1 ubiquitination by CRL3Structure (London, England : 1993) · 2025
    Article
  13. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. An expanded lexicon for the ubiquitin code.Nature reviews. Molecular cell biology · 2023
    Review
  18. Article
  19. Article
  20. Article

14 more citing papers are in PubMed but not listed here.

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

10 authors.

Ian R Kelsall1] Scottish Institute for Cell Signalling, College of Life Sciences, University of Dundee, Dundee, UK [2] Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, UK.
David M Duda
Jennifer L Olszewski
Axel Knebel
Frédéric Langevin
Nicola Wood
Melanie Wightman
Brenda A Schulman
Arno F Alpi

Funding

Ubiquitin-like Protein Transfer CascadesR01GM069530 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2003 to 2013
$3.4M
Structure and Mechanism of the Parkin Ubiquitin LigaseR03AG022633 · NIA · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2003 to 2003
$75k
Howard Hughes Medical InstituteNIA NIH HHS R03 AG022633NIGMS NIH HHS R01GM065930NIGMS NIH HHS R01 GM069530Wellcome TrustWellcome Trust 097945/B/11/Z
6 · The paper itself

Abstract

RING (Really Interesting New Gene)-in-between-RING (RBR) enzymes are a distinct class of E3 ubiquitin ligases possessing a cluster of three zinc-binding domains that cooperate to catalyse ubiquitin transfer. The regulation and biological function for most members of the RBR ligases is not known, and all RBR E3s characterized to date are auto-inhibited for in vitro ubiquitylation. Here, we show that TRIAD1 and HHARI, two members of the Ariadne subfamily ligases, associate with distinct neddylated Cullin-RING ligase (CRL) complexes. In comparison to the modest E3 ligase activity displayed by isolated TRIAD1 or HHARI, binding of the cognate neddylated CRL to TRIAD1 or HHARI greatly stimulates RBR ligase activity in vitro, as determined by auto-ubiquitylation, their ability to stimulate dissociation of a thioester-linked UBCH7∼ubiquitin intermediate, and reactivity with ubiquitin-vinyl methyl ester. Moreover, genetic evidence shows that RBR ligase activity impacts both the levels and activities of neddylated CRLs in vivo. Cumulatively, our work proposes a conserved mechanism of CRL-induced Ariadne RBR ligase activation and further suggests a reciprocal role of this special class of RBRs as regulators of distinct CRLs.

Indexed as

Carrier ProteinsCullin ProteinsCyclopentanesHEK293 CellsHumansNEDD8 ProteinPyrimidinesUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitinsARIH1 protein, humanARIH2 protein, humanCarrier ProteinsCUL5 protein, humanCullin ProteinsCyclopentanesNEDD8 ProteinNEDD8 protein, humanpevonedistatPyrimidinesUBE2L3 protein, humanUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID24076655
PMCPMC3817463

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.