Evidence map›Paper›PMID 26449534›Full record

ArticleScientific reports2015

Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly.

Vladyslava Sokolova, Frances Li, George Polovin, Soyeon Park

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
1.7field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Proteasome and Its Network: Engineering for Adaptability.Cold Spring Harbor perspectives in biology · 2020
    Review
  15. Article
  16. Article
  17. Ubiquitin-dependent switch during assembly of the proteasomal ATPases mediated by Not4 ubiquitin ligase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Regulation of proteasome assembly and activity in health and disease.Nature reviews. Molecular cell biology · 2018
    Review
  19. Review
  20. Proteasome Structure and Assembly.Journal of molecular biology · 2017
    Review
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

4 authors at 1 institution in 1 country.

Vladyslava SokolovaDepartment of Molecular, Cellular, and Developmental Biology University of Colorado, Boulder, CO 80309.
Frances LiDepartment of Molecular, Cellular, and Developmental Biology University of Colorado, Boulder, CO 80309.
George PolovinDepartment of Molecular, Cellular, and Developmental Biology University of Colorado, Boulder, CO 80309.
Soyeon ParkDepartment of Molecular, Cellular, and Developmental Biology University of Colorado, Boulder, CO 80309.
University of Colorado Boulder · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the proteasome, the proteolytic 20S core particle (CP) associates with the 19S regulatory particle (RP) to degrade polyubiquitinated proteins. Six ATPases (Rpt1-Rpt6) of the RP form a hexameric Rpt ring and interact with the heptameric α ring (α1-α7) of the CP via the Rpt C-terminal tails individually binding to the α subunits. Importantly, the Rpt6 tail has been suggested to be crucial for RP assembly. Here, we show that the interaction of the CP and Rpt6 tail promotes a CP-Rpt3 tail interaction, and that they jointly mediate proteasome activation via opening the CP gate for substrate entry. The Rpt6 tail forms a novel relationship with the Nas6 chaperone, which binds to Rpt3 and regulates the CP-Rpt3 tail interaction, critically influencing cell growth and turnover of polyubiquitinated proteins. CP-Rpt6 tail binding promotes the release of Nas6 from the proteasome. Based on disulfide crosslinking that detects cognate α3-Rpt6 tail and α2-Rpt3 tail interactions in the proteasome, decreased α3-Rpt6 tail interaction facilitates robust α2-Rpt3 tail interaction that is also strongly ATP-dependent. Together, our data support the reported role of Rpt6 during proteasome assembly, and suggest that its function switches from anchoring for RP assembly into promoting Rpt3-dependent activation of the mature proteasome.

Indexed as

Adenosine TriphosphatasesBinding SitesImmunoblottingModels, MolecularMolecular ChaperonesMutationProteasome Endopeptidase ComplexProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTemperatureUbiquitinated ProteinsAdenosine TriphosphatasesMolecular ChaperonesNAS6 protein, S cerevisiaeProteasome Endopeptidase ComplexRpt3 protein, S cerevisiaeRPT6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinated Proteins

Identifiers

PMID26449534
PMCPMC4598862
OpenAlexW2412832033

What OpenQuestion holds

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LicenceCC BY
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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.