Evidence map›Paper›PMID 23535662›Full record

ArticleNature communications2013

CSN- and CAND1-dependent remodelling of the budding yeast SCF complex.

Aleksandra Zemla, Yann Thomas, Sylwia Kedziora, Axel Knebel, Nicola T Wood, Gwenaël Rabut, Thimo Kurz

Open access · hybridAbstract read
PubMed Publisher
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
6.3field-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

65 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review: A silent concert in developing plants: Dynamic assembly of cullin-RING ubiquitin ligases.Plant science : an international journal of experimental plant biology · 2023
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. CAND1 is required for pollen viability inFrontiers in plant science · 2022
    Article
  13. Quantitative analyses for effects of neddylation on CRL2Protein science : a publication of the Protein Society · 2021
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Aleksandra ZemlaScottish Institute for Cell Signalling, Protein Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee, Scotland, UK.
Yann Thomas
Sylwia Kedziora
Axel Knebel
Nicola T Wood
Gwenaël Rabut
Thimo Kurz
University of Dundee · GBInstitut de génétique et de développement de Rennes · FR

Funding

Medical Research Council MC_UU_12016/7
6 · The paper itself

Abstract

Cullin-RING ligases (CRLs) are ubiquitin E3 enzymes with variable substrate-adaptor and -receptor subunits. All CRLs are activated by modification of the cullin subunit with the ubiquitin-like protein Nedd8 (neddylation). The protein CAND1 (Cullin-associated-Nedd8-dissociated-1) also promotes CRL activity, even though it only interacts with inactive ligase complexes. The molecular mechanism underlying this behaviour remains largely unclear. Here, we find that yeast SCF (Skp1-Cdc53-F-box) Cullin-RING complexes are remodelled in a CAND1-dependent manner, when cells are switched from growth in fermentable to non-fermentable carbon sources. Mechanistically, CAND1 promotes substrate adaptor release following SCF deneddylation by the COP9 signalosome (CSN). CSN- or CAND1-mutant cells fail to release substrate adaptors. This delays the formation of new complexes during SCF reactivation and results in substrate degradation defects. Our results shed light on how CAND1 regulates CRL activity and demonstrate that the cullin neddylation-deneddylation cycle is not only required to activate CRLs, but also to regulate substrate specificity through dynamic substrate adaptor exchange.

Indexed as

CarbonSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarbonSaccharomyces cerevisiae Proteins

Identifiers

PMID23535662
OpenAlexW1986128576

What OpenQuestion holds

Textmetadata
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.