Evidence map›Paper›PMID 25919710›Full record

ArticlePLoS genetics2015

The protein quality control machinery regulates its misassembled proteasome subunits.

Lee Zeev Peters, Ofri Karmon, Galit David-Kadoch, Rotem Hazan, Tzenlin Yu, Michael H Glickman, Shay Ben-Aroya

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 60 citations in OpenAlex.

  1. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Design principles that protect the proteasome from self-destruction.Protein science : a publication of the Protein Society · 2022
    Article
  8. Protein clearance strategies for disease intervention.Journal of neural transmission (Vienna, Austria : 1996) · 2022
    Review
  9. Article
  10. Article
  11. p62-containing, proteolytically active nuclear condensates, increase the efficiency of the ubiquitin-proteasome system.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
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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

7 authors at 2 institutions in 1 country.

Lee Zeev PetersFaculty of Life Sciences Bar-Ilan University, Ramat-Gan, Israel.
Ofri KarmonFaculty of Life Sciences Bar-Ilan University, Ramat-Gan, Israel.
Galit David-KadochFaculty of Life Sciences Bar-Ilan University, Ramat-Gan, Israel.
Rotem HazanFaculty of Life Sciences Bar-Ilan University, Ramat-Gan, Israel.
Tzenlin YuDepartement of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Michael H GlickmanDepartement of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Shay Ben-AroyaFaculty of Life Sciences Bar-Ilan University, Ramat-Gan, Israel.
Bar-Ilan University · ILTechnion – Israel Institute of Technology · IL

Funding

NIDA NIH HHS L60 DA052010
6 · The paper itself

Abstract

Cellular toxicity introduced by protein misfolding threatens cell fitness and viability. Failure to eliminate these polypeptides is associated with various aggregation diseases. In eukaryotes, the ubiquitin proteasome system (UPS) plays a vital role in protein quality control (PQC), by selectively targeting misfolded proteins for degradation. While the assembly of the proteasome can be naturally impaired by many factors, the regulatory pathways that mediate the sorting and elimination of misassembled proteasomal subunits are poorly understood. Here, we reveal how the dysfunctional proteasome is controlled by the PQC machinery. We found that among the multilayered quality control mechanisms, UPS mediated degradation of its own misassembled subunits is the favored pathway. We also demonstrated that the Hsp42 chaperone mediates an alternative pathway, the accumulation of these subunits in cytoprotective compartments. Thus, we show that proteasome homeostasis is controlled through probing the level of proteasome assembly, and the interplay between UPS mediated degradation or their sorting into distinct cellular compartments.

Indexed as

Genetic FitnessCell SurvivalHeat-Shock ProteinsProteasome Endopeptidase ComplexProtein FoldingProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationHeat-Shock ProteinsHSP42 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUbiquitin

Identifiers

PMID25919710
PMCPMC4412499
OpenAlexW2069828412

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.