Evidence map›Paper›PMID 24071738›Full record

ArticleNature communications2013

OTUB1 enhances TGFβ signalling by inhibiting the ubiquitylation and degradation of active SMAD2/3.

Lina Herhaus, Mazin Al-Salihi, Thomas Macartney, Simone Weidlich, Gopal P Sapkota

Open access · hybridAbstract read
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 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

93 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. TBK1 restricts IRGQ-mediated autophagy.Nature communications · 2026
    Article
  6. Article
  7. A viral Cyclin D homolog protein hijacks the metabolic stress sensor SESN2 to promote primary effusion lymphoma growth.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Review
  11. The SOX18-OTUB1-YAP1 axis: a new endometriosis target.Journal of translational medicine · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review

33 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

5 authors at 2 institutions in 1 country.

Lina HerhausMRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5 EH, Scotland, UK.
Mazin Al-Salihi
Thomas Macartney
Simone Weidlich
Gopal P Sapkota
University of Dundee · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Medical Research Council MC_U127092717Medical Research Council MC_UU_12016/3
6 · The paper itself

Abstract

SMAD transcription factors are key intracellular transducers of TGFβ cytokines. SMADs are tightly regulated to ensure balanced cellular responses to TGFβ signals. Ubiquitylation has a key role in regulating SMAD stability and activity. Several E3 ubiquitin ligases that regulate the turnover of SMADs are known; however, proteins that prevent the ubiquitylation or cause deubiquitylation of active SMADs remain undefined. Here we demonstrate that OTUB1 is recruited to the active phospho-SMAD2/3 complex only on TGFβ induction. Further, OTUB1 has a crucial role in TGFβ-mediated gene transcription and cellular migration. OTUB1 inhibits the ubiquitylation of phospho-SMAD2/3 by binding to and inhibiting the E2 ubiquitin-conjugating enzymes independent of its catalytic activity. Consequently, depletion of OTUB1 in cells causes a rapid loss in levels of TGFβ-induced phospho-SMAD2/3, which is rescued by the proteasomal inhibitor bortezomib. Our findings uncover a signal-induced phosphorylation-dependent recruitment of OTUB1 to its target in the TGFβ pathway.

Indexed as

AnimalsBoronic AcidsBortezomibCell Line, TumorCysteine EndopeptidasesDeubiquitinating EnzymesGene Expression RegulationGenes, ReporterGreen Fluorescent ProteinsHumansMicePhosphoproteinsPhosphorylationPrimary Cell CultureProteasome Endopeptidase ComplexProteasome InhibitorsBoronic AcidsBortezomibCysteine EndopeptidasesDeubiquitinating EnzymesGreen Fluorescent ProteinsOTUB1 protein, humanPhosphoproteinsProteasome Endopeptidase ComplexProteasome InhibitorsPyrazinesSmad2 ProteinSMAD2 protein, humanSmad3 ProteinSMAD3 protein, humanTransforming Growth Factor betaUbiquitin

Identifiers

PMID24071738
PMCPMC3791481
OpenAlexW2037407781

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.