Evidence map›Paper›PMID 21816351›Full record

ArticleMolecular cell2011

The TFIIH subunit Tfb3 regulates cullin neddylation.

Gwenaël Rabut, Gaëlle Le Dez, Rati Verma, Taras Makhnevych, Axel Knebel, Thimo Kurz, Charles Boone, Raymond J Deshaies, Matthias Peter

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

33 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Biomolecules · 2021
    Article
  11. Advances in Cancer Treatment by Targeting the Neddylation Pathway.Frontiers in cell and developmental biology · 2021
    Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Neddylation, a novel paradigm in liver cancer.Translational gastroenterology and hepatology · 2018
    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

9 authors at 5 institutions in 5 countries.

Gwenaël RabutInstitute of Biochemistry, ETH Zurich, Zurich, Switzerland. gwenael.rabut@univ-rennes1.fr
Gaëlle Le Dez
Rati Verma
Taras Makhnevych
Axel Knebel
Thimo Kurz
Charles Boone
Raymond J Deshaies
Matthias Peter
California Institute of Technology · USUniversité Européenne de Bretagne · FRUniversity of Dundee · GBUniversity of Toronto · CAETH Zurich · CH

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Cullin proteins are scaffolds for the assembly of multisubunit ubiquitin ligases, which ubiquitylate a large number of proteins involved in widely varying cellular functions. Multiple mechanisms cooperate to regulate cullin activity, including neddylation of their C-terminal domain. Interestingly, we found that the yeast Cul4-type cullin Rtt101 is not only neddylated but also ubiquitylated, and both modifications promote Rtt101 function in vivo. Surprisingly, proper modification of Rtt101 neither correlated with catalytic activity of the RING domain of Hrt1 nor required the Nedd8 ligase Dcn1. Instead, ubiquitylation of Rtt101 was dependent on the ubiquitin-conjugating enzyme Ubc4, while efficient neddylation involves the RING domain protein Tfb3, a subunit of the transcription factor TFIIH. Tfb3 also controls Cul3 neddylation and activity in vivo, and physically interacts with Ubc4 and the Nedd8-conjugating enzyme Ubc12 and the Hrt1/Rtt101 complex. Together, these results suggest that the conserved RING domain protein Tfb3 controls activation of a subset of cullins.

Indexed as

Cullin ProteinsMutationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSKP Cullin F-Box Protein LigasesTranscription Factors, TFIITranscription Factor TFIIHUbiquitinationUbiquitin-Protein LigasesUbiquitinsCdc53 protein, S cerevisiaeCullin ProteinsDcn1 protein, S cerevisiaeHRT1 protein, S cerevisiaeRTT101 protein, S cerevisiaeRUB1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSKP Cullin F-Box Protein LigasesTFB3 protein, S cerevisiaeTranscription Factors, TFIITranscription Factor TFIIHUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID21816351
PMCPMC3186349
OpenAlexW2066454074

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.