Evidence map›Paper›PMID 25812915›Full record

ArticleNature communications2015

Maturation of the proteasome core particle induces an affinity switch that controls regulatory particle association.

Prashant S Wani, Michael A Rowland, Alex Ondracek, Eric J Deeds, Jeroen Roelofs

Abstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mechanism of autocatalytic activation during proteasome assembly.Nature structural & molecular biology · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Yeast PI31 inhibits the proteasome by a direct multisite mechanism.Nature structural & molecular biology · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

5 authors.

Prashant S WaniGraduate Biochemistry Group, Department of Biochemistry and Molecular Biophysics, Kansas State University, 336 Ackert Hall, Manhattan, Kansas 66506, USA.
Michael A RowlandCenter for Computational Biology, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047, USA.
Alex OndracekMolecular, Cellular and Developmental Biology Program, Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, Kansas 66506, USA.
Eric J Deeds1] Center for Computational Biology, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047, USA [2] Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66047, USA [3] Santa Fe Institute, Santa Fe, New Mexico 87501, USA.
Jeroen Roelofs1] Graduate Biochemistry Group, Department of Biochemistry and Molecular Biophysics, Kansas State University, 336 Ackert Hall, Manhattan, Kansas 66506, USA [2] Molecular, Cellular and Developmental Biology Program, Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, Kansas 66506, USA.ORCID 0000000309442465

Funding

Mentoring CoreP20GM103418 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI SUSAN J. BROWN · 2012 to 2026
$63.0M
TRAFFICKING OF THE PLASMA MEMBRANE CA2+-ATPASE TO RAFTSP20RR017708 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI HOLYOAK, TODD · 2002 to 2011
$20.1M
Protein Structure and FunctionP20GM103420 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2012 to 2012
$2.0M
Allosteric Mechanisms Controlling the Formation of Different Proteasome ComplexesR15GM112142 · NIGMS · KANSAS STATE UNIVERSITY · PI ROELOFS, JEROEN · 2015 to 2015
$360k
NCRR NIH HHS P20 RR017708NIGMS NIH HHS P20 GM103418NIGMS NIH HHS P20GM103418NIGMS NIH HHS P20 GM103420NIGMS NIH HHS P20GM103420NIGMS NIH HHS R15 GM112142
6 · The paper itself

Abstract

Proteasome assembly is a complex process, requiring 66 subunits distributed over several subcomplexes to associate in a coordinated fashion. Ten proteasome-specific chaperones have been identified that assist in this process. For two of these, the Pba1-Pba2 dimer, it is well established that they only bind immature core particles (CPs) in vivo. In contrast, the regulatory particle (RP) utilizes the same binding surface but only interacts with the mature CP in vivo. It is unclear how these binding events are regulated. Here, we show that Pba1-Pba2 binds tightly to the immature CP, preventing RP binding. Changes in the CP that occur on maturation significantly reduce its affinity for Pba1-Pba2, enabling the RP to displace the chaperone. Mathematical modelling indicates that this 'affinity switch' mechanism has likely evolved to improve assembly efficiency by preventing the accumulation of stable, non-productive intermediates. Our work thus provides mechanistic insights into a crucial step in proteasome biogenesis.

Indexed as

Protein Structure, QuaternaryElectrophoresis, Gel, Two-DimensionalModels, MolecularModels, TheoreticalMolecular ChaperonesProteasome Endopeptidase ComplexProtein BindingSaccharomyces cerevisiae ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationMolecular ChaperonesPba1 protein, S cerevisiaePba2 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae Proteins

Identifiers

PMID25812915
PMCPMC4380239

What OpenQuestion holds

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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.