Evidence map›Paper›PMID 21289098›Full record

ArticleMolecular biology of the cell2011

Dual function of Rpn5 in two PCI complexes, the 26S proteasome and COP9 signalosome.

Zanlin Yu, Oded Kleifeld, Avigail Lande-Atir, Maisa Bsoul, Maya Kleiman, Daria Krutauz, Adam Book, Richard D Vierstra, Kay Hofmann, Noa Reis and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Csn5 Depletion Reverses Mitochondrial Defects in GCN5-NullInternational journal of molecular sciences · 2025
    Article
  3. Article
  4. The Ubiquitin-like Proteins ofBiomolecules · 2023
    Review
  5. Strategies for Monitoring "Ubiquitin C-Terminal Hydrolase 1" (Yuh1) Activity.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. Review
  7. Biomolecules · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Proteasome Structure and Assembly.Journal of molecular biology · 2017
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. The NEDD8 modification pathway in plants.Frontiers in plant science · 2014
    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

12 authors at 5 institutions in 3 countries.

Zanlin YuDepartment of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel.
Oded Kleifeld
Avigail Lande-Atir
Maisa Bsoul
Maya Kleiman
Daria Krutauz
Adam Book
Richard D Vierstra
Kay Hofmann
Noa Reis
Michael H Glickman
Elah Pick
Technion – Israel Institute of Technology · ILUniversity of Wisconsin–Madison · USMiltenyi Biotec (Germany) · DEOranim Academic College of Education · ILUniversity of Haifa · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Subunit composition and architectural structure of the 26S proteasome lid is strictly conserved between all eukaryotes. This eight-subunit complex bears high similarity to the eukaryotic translation initiation factor 3 and to the COP9 signalosome (CSN), which together define the proteasome CSN/COP9/initiation factor (PCI) troika. In some unicellular eukaryotes, the latter two complexes lack key subunits, encouraging questions about the conservation of their structural design. Here we demonstrate that, in Saccharomyces cerevisiae, Rpn5 plays dual roles by stabilizing proteasome and CSN structures independently. Proteasome and CSN complexes are easily dissected, with Rpn5 the only subunit in common. Together with Rpn5, we identified a total of six bona fide subunits at roughly stoichiometric ratios in isolated, affinity-purified CSN. Moreover, the copy of Rpn5 associated with the CSN is required for enzymatic hydrolysis of Rub1/Nedd8 conjugated to cullins. We propose that multitasking by a single subunit, Rpn5 in this case, allows it to function in different complexes simultaneously. These observations demonstrate that functional substitution of subunits by paralogues is feasible, implying that the canonical composition of the three PCI complexes in S. cerevisiae is more robust than hitherto appreciated.

Indexed as

COP9 Signalosome ComplexCullin ProteinsMolecular WeightMultiprotein ComplexesPeptide HydrolasesPhenotypeProteasome Endopeptidase ComplexProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATP dependent 26S proteaseCOP9 Signalosome ComplexCullin ProteinsMultiprotein ComplexesPeptide HydrolasesProteasome Endopeptidase ComplexProtein SubunitsRpn5 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID21289098
PMCPMC3069016
OpenAlexW2171858691

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.