Evidence map›Paper›PMID 24613342›Full record

ArticleMolecular cell2014

Ubiquitin signals proteolysis-independent stripping of transcription factors.

Ada Ndoja, Robert E Cohen, Tingting Yao

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Fast friends - Ubiquitin-like modifiers as engineered fusion partners.Seminars in cell & developmental biology · 2022
    Review
  5. Article
  6. Article
  7. USP7 and VCPCell reports · 2021
    Article
  8. Article
  9. Review
  10. Review
  11. The ubiquitin system affects agronomic plant traits.The Journal of biological chemistry · 2020
    Review
  12. Cdc48 cofactor Shp1 regulates signal-induced SCFProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ada NdojaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA.
Robert E CohenDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA.
Tingting YaoDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA. Electronic address: tingting.yao@colostate.edu.
Colorado State University · US

Funding

Regulation of a Deubiquitinating Enzyme in Proteolysis and Chromatin RemodelingR01GM098401 · NIGMS · COLORADO STATE UNIVERSITY · PI YAO, TINGTING · 2011 to 2021
$2.9M
Linkage-specific recognition of polyubiquitinR01GM097452 · NIGMS · COLORADO STATE UNIVERSITY · PI COHEN, ROBERT · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM097452NIGMS NIH HHS R01GM097452NIGMS NIH HHS R01 GM098401NIGMS NIH HHS R01GM098401
6 · The paper itself

Abstract

Ubiquitination of transcription activators has been reported to regulate transcription via both proteolytic and nonproteolytic routes, yet the function of the ubiquitin (Ub) signal in the nonproteolytic process is poorly understood. By use of the heterologous transcription activator LexA-VP16 in Saccharomyces cerevisiae, we show that monoubiquitin fusion of the activator prevents stable interactions between the activator and DNA, leading to transcription inhibition without activator degradation. We identify the AAA(+) ATPase Cdc48 and its cofactors as the Ub receptor responsible for extracting the monoubiquitinated activator from DNA. Our results suggest that deubiquitination of the activator is critical for transcription activation. These findings with LexA-VP16 extend in both yeast and mammalian cells to native transcription activators Met4 and R-Smads, respectively, that are known to be oligo-ubiquitinated. The results illustrate a role for Ub and Cdc48 in transcriptional regulation and gene expression that is independent of proteolysis.

Indexed as

Transcriptional ActivationAdenosine TriphosphatasesBasic-Leucine Zipper Transcription FactorsBinding SitesCell Cycle ProteinsCell Line, TumorDNAHumansNuclear ProteinsProtein BindingProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSmad Proteins, Receptor-RegulatedTranscription, GeneticAdenosine TriphosphatasesBasic-Leucine Zipper Transcription FactorsCDC48 protein, S cerevisiaeCell Cycle ProteinsDNAMET4 protein, S cerevisiaenuclear protein import factor p97Nuclear ProteinsSaccharomyces cerevisiae ProteinsSmad Proteins, Receptor-RegulatedUbiquitinValosin Containing Protein

Identifiers

PMID24613342
PMCPMC4005849
OpenAlexW2085196189

What OpenQuestion holds

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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.