Evidence map›Paper›PMID 32978409›Full record

ArticleScientific reports2020

Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins.

Joanna Abi Habib, Etienne De Plaen, Vincent Stroobant, Dusan Zivkovic, Marie-Pierre Bousquet, Benoît Guillaume, Khadija Wahni, Joris Messens, Antonia Busse, Nathalie Vigneron and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. 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
2.3field-weighted citation impact, top 11% 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, 53 citations in OpenAlex.

  1. Article
  2. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
  3. Observational
  4. Article
  5. Review
  6. Review
  7. Article
  8. Tracking proteasome degradation: A cross-organ analysis via intact degradomics mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Therapeutic potential of zincFrontiers in pharmacology · 2025
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Regulation of P-Glycoprotein during Oxidative Stress.Antioxidants (Basel, Switzerland) · 2024
    Review
  19. Review
  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

11 authors at 4 institutions in 4 countries.

Joanna Abi HabibLudwig Institute for Cancer Research, Brussels, 1200, Belgium.ORCID http://orcid.org/0000-0002-9920-6927
Etienne De PlaenLudwig Institute for Cancer Research, Brussels, 1200, Belgium.
Vincent StroobantLudwig Institute for Cancer Research, Brussels, 1200, Belgium.
Dusan ZivkovicInstitut de Pharmacologie et Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France.ORCID http://orcid.org/0000-0001-5794-4422
Marie-Pierre BousquetInstitut de Pharmacologie et Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France.ORCID http://orcid.org/0000-0003-2680-8932
Benoît GuillaumeLudwig Institute for Cancer Research, Brussels, 1200, Belgium.
Khadija WahniStructural Biology Research Center, VIB, 1050, Brussels, Belgium.
Joris MessensStructural Biology Research Center, VIB, 1050, Brussels, Belgium.ORCID http://orcid.org/0000-0002-2128-8264
Antonia BusseMedizinische Klinik III, Hämatologie, Onkologie und Tumorimmunologie Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität Zu Berlin, and Berlin Institute of Health, Campus Benjamin Franklin, Hindenburgdamm 30, 12203, Berlin, Germany.
Nathalie Vigneron *Ludwig Institute for Cancer Research, Brussels, 1200, Belgium. nathalie.vigneron@bru.licr.org.ORCID http://orcid.org/0000-0002-2761-2803
Benoit J Van den Eynde *Ludwig Institute for Cancer Research, Brussels, 1200, Belgium. benoit.vandeneynde@bru.licr.org.ORCID http://orcid.org/0000-0002-4995-3270
Ludwig Cancer Research · BECentre National de la Recherche Scientifique · FRVrije Universiteit Brussel · BEGerman Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteasome is responsible for selective degradation of proteins. It exists in mammalian cells under four main subtypes, which differ by the combination of their catalytic subunits: the standard proteasome (β1-β2-β5), the immunoproteasome (β1i-β2i-β5i) and the two intermediate proteasomes (β1-β2-β5i and β1i-β2-β5i). The efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins remains unclear. Using cells expressing exclusively one proteasome subtype, we observed that ubiquitinated p21 and c--myc were degraded at similar rates, indicating that the four 26S proteasomes degrade ubiquitinated proteins equally well. Under oxidative stress, we observed a partial dissociation of 26S into 20S proteasomes, which can degrade non-ubiquitinated oxidized proteins. Oxidized calmodulin and hemoglobin were best degraded in vitro by the three β5i-containing 20S proteasomes, while their native forms were not degraded. Circular dichroism analyses indicated that ubiquitin-independent recognition of oxidized proteins by 20S proteasomes was triggered by the disruption of their structure. Accordingly, β5i-containing 20S proteasomes degraded unoxidized naturally disordered protein tau, while 26S proteasomes did not. Our results suggest that the three β5i-containing 20S proteasomes, namely the immunoproteasome and the two intermediate proteasomes, might help cells to eliminate proteins containing disordered domains, including those induced by oxidative stress.

Indexed as

ProteolysisUbiquitinationCyclin-Dependent Kinase Inhibitor p21HEK293 CellsHumansOxidation-ReductionProteasome Endopeptidase ComplexProto-Oncogene Proteins c-mycCyclin-Dependent Kinase Inhibitor p21MYC protein, humanProteasome Endopeptidase ComplexProto-Oncogene Proteins c-myc

Identifiers

PMID32978409
PMCPMC7519072
OpenAlexW3088231900

What Socratic 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 Socratic graph.