Evidence map›Paper›PMID 34702852›Full record

ArticleNature communications2021

The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag.

Indrajit Sahu, Sachitanand M Mali, Prasad Sulkshane, Cong Xu, Andrey Rozenberg, Roni Morag, Manisha Priyadarsini Sahoo, Sumeet K Singh, Zhanyu Ding, Yifan Wang and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
7.8field-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

86 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
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  6. Identification of a Ubiquitin-Independent Degron by a Reporter Assay.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Article
  8. Review
  9. Article
  10. Molecular mechanisms underlying p62-dependent secretion of the Alzheimer-associated ubiquitin variant UBBProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. An anti-adhesive peptide found in extracellular vesicles fromCell surface (Amsterdam, Netherlands) · 2025
    Article
  12. Article
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  15. Review
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26 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

15 authors at 3 institutions in 3 countries.

Indrajit SahuFaculty of Biology, Technion-Israel Institute of Technology, Haifa, 32000, Israel.ORCID http://orcid.org/0000-0002-4143-0600
Sachitanand M MaliSchulich faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, 32000, Israel.
Prasad SulkshaneFaculty of Biology, Technion-Israel Institute of Technology, Haifa, 32000, Israel.
Cong XuState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, China.
Andrey RozenbergFaculty of Biology, Technion-Israel Institute of Technology, Haifa, 32000, Israel.
Roni MoragFaculty of Biology, Technion-Israel Institute of Technology, Haifa, 32000, Israel.
Manisha Priyadarsini SahooFaculty of Biology, Technion-Israel Institute of Technology, Haifa, 32000, Israel.
Sumeet K SinghSchulich faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, 32000, Israel.
Zhanyu DingState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, China.
Yifan WangState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, China.ORCID http://orcid.org/0000-0001-9966-682X
Sharleen DayDepartment of Medicine, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Yao CongState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, China.ORCID http://orcid.org/0000-0002-7164-8694
Oded KleifeldFaculty of Biology, Technion-Israel Institute of Technology, Haifa, 32000, Israel. okleifeld@technion.ac.il.ORCID http://orcid.org/0000-0003-3091-7154
Ashraf BrikSchulich faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, 32000, Israel. abrik@technion.ac.il.ORCID http://orcid.org/0000-0001-8745-2250
Michael H GlickmanFaculty of Biology, Technion-Israel Institute of Technology, Haifa, 32000, Israel. glickman@technion.ac.il.ORCID http://orcid.org/0000-0002-1222-8104
Technion – Israel Institute of Technology · ILChinese Academy of Sciences · CNUniversity of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteasome, the primary protease for ubiquitin-dependent proteolysis in eukaryotes, is usually found as a mixture of 30S, 26S, and 20S complexes. These complexes have common catalytic sites, which makes it challenging to determine their distinctive roles in intracellular proteolysis. Here, we chemically synthesize a panel of homogenous ubiquitinated proteins, and use them to compare 20S and 26S proteasomes with respect to substrate selection and peptide-product generation. We show that 20S proteasomes can degrade the ubiquitin tag along with the conjugated substrate. Ubiquitin remnants on branched peptide products identified by LC-MS/MS, and flexibility in the 20S gate observed by cryo-EM, reflect the ability of the 20S proteasome to proteolyze an isopeptide-linked ubiquitin-conjugate. Peptidomics identifies proteasome-trapped ubiquitin-derived peptides and peptides of potential 20S substrates in Hi20S cells, hypoxic cells, and human failing-heart. Moreover, elevated levels of 20S proteasomes appear to contribute to cell survival under stress associated with damaged proteins.

Indexed as

Cell HypoxiaCell SurvivalHeart FailureHumansPeptidesProteasome Endopeptidase ComplexProtein ConformationProteolysisSubstrate SpecificityUbiquitinUbiquitinated ProteinsUbiquitinationPeptidesProteasome Endopeptidase ComplexUbiquitinUbiquitinated Proteins

Identifiers

PMID34702852
PMCPMC8548400
OpenAlexW3210198252

What OpenQuestion holds

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Registered trials

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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.