Evidence map›Paper›PMID 26906416›Full record

ArticleJournal of cell science2016

Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.

Matthew J Keuss, Yann Thomas, Robin Mcarthur, Nicola T Wood, Axel Knebel, Thimo Kurz

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. DCUN1D2 is insignificant for spermatogenesis and male fertility in mice.American journal of translational research · 2025
    Article
  7. Dcun1d3 is dispensable for spermatogenesis and male fertility in mice.American journal of clinical and experimental immunology · 2025
    Article
  8. Article
  9. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Whole transcriptome analysis of platelet concentrates during storage.Blood transfusion = Trasfusione del sangue · 2023
    Article
  15. Article
  16. Review
  17. Article
  18. WNK4 kinase: from structure to physiology.American journal of physiology. Renal physiology · 2021
    Review
  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

6 authors at 3 institutions in 1 country.

Matthew J KeussMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Yann ThomasMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Robin McarthurMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Nicola T WoodMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Axel KnebelMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Thimo KurzMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK thimo.kurz@glasgow.ac.uk.
MRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GBMedical Research Council · GB

Funding

European Research Council 243019Medical Research Council MC_UU_12016/7
6 · The paper itself

Abstract

Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. DCNs are NEDD8 E3 ligases that promote neddylation. Mammalian cells express five DCN-like (DCNL) proteins but little is known about their specific functions or interaction partners. We found that DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor. These CAND-cullin-DCNL complexes might represent 'reserve' CRLs that can be rapidly activated when needed. We further found that all DCNLs interact with most cullin subtypes, but that they are probably responsible for the neddylation of different subpopulations of any given cullin. This is consistent with the fact that the subcellular localization of DCNLs in tissue culture cells differs and that they show unique tissue-specific expression patterns in mice. Thus, the specificity between DCNL-type NEDD8 E3 enzymes and their cullin substrates is only apparent in well-defined physiological contexts and related to their subcellular distribution and restricted expression.

Indexed as

Cell Cycle ProteinsCell LineCullin ProteinsHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsNEDD8 ProteinOncogene ProteinsPeptide SynthasesProtein BindingProteinsProto-Oncogene ProteinsRNA InterferenceRNA, Small InterferingTranscription FactorsUbiquitin-Protein LigasesCAND1 protein, humanCell Cycle ProteinsCullin ProteinsCULL-RING ligase, humanDCUN1D1 protein, humanDCUN1D3 protein, humanDCUN1D5 protein, humanIntracellular Signaling Peptides and ProteinsNEDD8 ProteinNEDD8 protein, humanOncogene ProteinsPeptide SynthasesProteinsProto-Oncogene ProteinsRNA, Small InterferingTranscription FactorsUbiquitin-Protein LigasesUbiquitinsCRLCullin-RING ligasesDCUN1DNEDD8SCCROUbiquitin

Identifiers

PMID26906416
PMCPMC4886823
OpenAlexW2274056677

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.