Evidence map›Paper›PMID 33974913›Full record

ArticleMolecular cell2021

Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase.

Ka-Yiu Edwin Kong, Bernd Fischer, Matthias Meurer, Ilia Kats, Zhaoyan Li, Frank Rühle, Joseph D Barry, Daniel Kirrmaier, Veronika Chevyreva, Bryan-Joseph San Luis and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.2field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025
    Review
  5. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. The hGIDLife science alliance · 2024
    Article
  10. Article
  11. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  12. Article
  13. Muskelin acts as a substrate receptor of the highly regulatedbioRxiv : the preprint server for biology · 2024
    Article
  14. Article
  15. Article
  16. Article
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  19. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 5 institutions in 2 countries.

Ka-Yiu Edwin KongInstitute of Molecular Biology (IMB), Mainz, Germany.
Bernd FischerComputational Genome Biology, German Cancer Research Center (DKFZ), Heidelberg, Germany.
Matthias MeurerCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Ilia KatsCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Zhaoyan LiInstitute of Molecular Biology (IMB), Mainz, Germany.
Frank RühleInstitute of Molecular Biology (IMB), Mainz, Germany.
Joseph D BarryGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Daniel KirrmaierCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany; Cell Morphogenesis and Signal Transduction, German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Veronika ChevyrevaCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany.
Bryan-Joseph San LuisThe Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON, Canada; Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada.
Michael CostanzoThe Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON, Canada; Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada.
Wolfgang HuberGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Brenda J AndrewsThe Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON, Canada; Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada.
Charles BooneThe Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON, Canada; Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada.
Michael KnopCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Heidelberg, Germany; Cell Morphogenesis and Signal Transduction, German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Heidelberg, Germany. Electronic address: m.knop@zmbh.uni-heidelberg.de.
Anton KhmelinskiiInstitute of Molecular Biology (IMB), Mainz, Germany. Electronic address: a.khmelinskii@imb-mainz.de.
Institute of Molecular Biology · DEUniversity of Toronto · CAGerman Cancer Research Center · DEHeidelberg University · DEEuropean Molecular Biology Laboratory · DE

Funding

Mapping the reference genetic network of a eukaryotic cellR01HG005853 · NHGRI · UNIVERSITY OF TORONTO · PI ANDREWS, BRENDA JEAN, BOONE, CHARLES · 2010 to 2025
$7.6M
CIHR FDN-143264CIHR FDN-143265NHGRI NIH HHS R01 HG005853
6 · The paper itself

Abstract

Selective protein degradation by the ubiquitin-proteasome system (UPS) is involved in all cellular processes. However, the substrates and specificity of most UPS components are not well understood. Here we systematically characterized the UPS in Saccharomyces cerevisiae. Using fluorescent timers, we determined how loss of individual UPS components affects yeast proteome turnover, detecting phenotypes for 76% of E2, E3, and deubiquitinating enzymes. We exploit this dataset to gain insights into N-degron pathways, which target proteins carrying N-terminal degradation signals. We implicate Ubr1, an E3 of the Arg/N-degron pathway, in targeting mitochondrial proteins processed by the mitochondrial inner membrane protease. Moreover, we identify Ylr149c/Gid11 as a substrate receptor of the glucose-induced degradation-deficient (GID) complex, an E3 of the Pro/N-degron pathway. Our results suggest that Gid11 recognizes proteins with N-terminal threonines, expanding the specificity of the GID complex. This resource of potential substrates and relationships between UPS components enables exploring functions of selective protein degradation.

Indexed as

Protein Processing, Post-TranslationalGene Expression ProfilingGene Expression Regulation, FungalGenes, ReporterGreen Fluorescent ProteinsLuminescent ProteinsMitochondrial ProteinsProteasome Endopeptidase ComplexProtein TransportProteolysisProteomicsRed Fluorescent ProteinSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThreonineUbiquitinGreen Fluorescent ProteinsLuminescent ProteinsMitochondrial ProteinsProteasome Endopeptidase ComplexRed Fluorescent ProteinSaccharomyces cerevisiae ProteinsThreonineUbiquitinUbiquitin-Protein LigasesUBR1 protein, S cerevisiaefluorescent timersGID ubiquitin ligaseN-degron pathwaysprotein quality controlproteostasisselective protein degradationubiquitin-proteasome system

Identifiers

PMID33974913
PMCPMC8189435
OpenAlexW3159215495

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.