Evidence map›Paper›PMID 19153604›Full record

ArticleThe EMBO journal2009

Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3.

Sokol V Todi, Brett J Winborn, K Matthew Scaglione, Jessica R Blount, Sue M Travis, Henry L Paulson

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed, 1 pooled it
5.9field-weighted citation impact, top 2% 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

101 citing papers in PubMed, 1 synthesis or guideline pooled it, 170 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Ubiquitin-modifying enzymes in Huntington's disease.Frontiers in molecular biosciences · 2023
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Cells · 2022
    Article
  20. Review

41 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

6 authors at 2 institutions in 1 country.

Sokol V TodiDepartment of Neurology, University of Michigan, Ann Arbor, MI 48109, USA.
Brett J Winborn
K Matthew Scaglione
Jessica R Blount
Sue M Travis
Henry L Paulson
University of Michigan–Ann Arbor · USUniversity of Iowa · US

Funding

Mechanisms of Polyglutamine NeurodegenerationR01NS038712 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PAULSON, HENRY L · 2000 to 2019
$8.1M
NINDS NIH HHS NS038712NINDS NIH HHS R01 NS038712
6 · The paper itself

Abstract

Deubiquitinating enzymes (DUBs) control the ubiquitination status of proteins in various cellular pathways. Regulation of the activity of DUBs, which is critically important to cellular homoeostasis, can be achieved at the level of gene expression, protein complex formation, or degradation. Here, we report that ubiquitination also directly regulates the activity of a DUB, ataxin-3, a polyglutamine disease protein implicated in protein quality control pathways. Ubiquitination enhances ubiquitin (Ub) chain cleavage by ataxin-3, but does not alter its preference for K63-linked Ub chains. In cells, ubiquitination of endogenous ataxin-3 increases when the proteasome is inhibited, when excess Ub is present, or when the unfolded protein response is induced, suggesting that the cellular functions of ataxin-3 in protein quality control are modulated through ubiquitination. Ataxin-3 is the first reported DUB in which ubiquitination directly regulates catalytic activity. We propose a new function for protein ubiquitination in regulating the activity of certain DUBs and perhaps other enzymes.

Indexed as

AnimalsAtaxin-3BrainCatalysisChlorocebus aethiopsCOS CellsGene Expression RegulationHomeostasisHumansMachado-Joseph DiseaseModels, BiologicalNerve Tissue ProteinsNuclear ProteinsProtein DenaturationProtein FoldingProtein Processing, Post-TranslationalAtaxin-3ATXN3 protein, humanNerve Tissue ProteinsNuclear ProteinsRepressor ProteinsUbiquitin

Identifiers

PMID19153604
PMCPMC2646149
OpenAlexW2136412949

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.