Evidence map›Paper›PMID 27234297›Full record

ArticleThe EMBO journal2016

Ubiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.

Houqing Yu, Grace Kago, Christopher M Yellman, Andreas Matouschek

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.0field-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

42 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  4. Article
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  6. The Dsc complex and its role in Golgi quality control.Biochemical Society transactions · 2024
    Review
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  9. Viable mutations of mouse midnolin suppress B cell malignancies.The Journal of experimental medicine · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. The Ubiquitin-like Proteins ofBiomolecules · 2023
    Review
  14. Article
  15. Article
  16. Applications and Limitations of Oxime-Linked "Split PROTACs".Chembiochem : a European journal of chemical biology · 2022
    Article
  17. Article
  18. Design principles that protect the proteasome from self-destruction.Protein science : a publication of the Protein Society · 2022
    Article
  19. Proteasomal conformation controls unfolding ability.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

4 authors at 2 institutions in 1 country.

Houqing YuDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA Department of Molecular Biosciences, Northwestern University, Evanston, IL, USA.
Grace KagoDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Christopher M YellmanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Andreas MatouschekDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA Department of Molecular Biosciences, Northwestern University, Evanston, IL, USA matouschek@austin.utexas.edu.ORCID 0000-0001-6016-2341
Northwestern University · USThe University of Texas at Austin · US

Funding

Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017
$3.7M
Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
Development of proteasome adaptors to catalytically deplete specific proteins from cellsR21CA196456 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI MATOUSCHEK, ANDREAS · 2016 to 2018
$597k
Cracking the Ubiquitination Code by Top Down Mass SpectrometryR21CA191664 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2015 to 2016
$355k
NCI NIH HHS R21 CA191664NCI NIH HHS R21 CA196456NIGMS NIH HHS R01 GM063004NIGMS NIH HHS U54 GM105816
6 · The paper itself

Abstract

Ubiquitin and some of its homologues target proteins to the proteasome for degradation. Other ubiquitin-like domains are involved in cellular processes unrelated to the proteasome, and proteins containing these domains remain stable in the cell. We find that the 10 yeast ubiquitin-like domains tested bind to the proteasome, and that all 11 identified domains can target proteins for degradation. Their apparent proteasome affinities are not directly related to their stabilities or functions. That is, ubiquitin-like domains in proteins not part of the ubiquitin proteasome system may bind the proteasome more tightly than domains in proteins that are bona fide components. We propose that proteins with ubiquitin-like domains have properties other than proteasome binding that confer stability. We show that one of these properties is the absence of accessible disordered regions that allow the proteasome to initiate degradation. In support of this model, we find that Mdy2 is degraded in yeast when a disordered region in the protein becomes exposed and that the attachment of a disordered region to Ubp6 leads to its degradation.

Indexed as

ProteolysisEndopeptidasesProteasome Endopeptidase ComplexProtein BindingProtein ConformationProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinEndopeptidasesMdy2 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUbiquitinUBP6 protein, S cerevisiaedegradationproteasomeubiquitin‐like domain

Identifiers

PMID27234297
PMCPMC4884787
OpenAlexW2400425908

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.