Evidence map›Paper›PMID 26451487›Full record

ArticleCell2015

A Single α Helix Drives Extensive Remodeling of the Proteasome Lid and Completion of Regulatory Particle Assembly.

Robert J Tomko, David W Taylor, Zhuo A Chen, Hong-Wei Wang, Juri Rappsilber, Mark Hochstrasser

Abstract read
In one paragraph

Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
–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

52 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
  5. Review
  6. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  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

6 authors.

Robert J TomkoDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. Electronic address: robert.tomko@med.fsu.edu.
David W TaylorCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720-3200, USA.
Zhuo A ChenWellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, King's Buildings, Max Born Crescent, Mayfield Road, Edinburgh EH9 3BF, Scotland.
Hong-Wei WangTsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, PRC.
Juri RappsilberWellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, King's Buildings, Max Born Crescent, Mayfield Road, Edinburgh EH9 3BF, Scotland; Department of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany.
Mark HochstrasserDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. Electronic address: mark.hochstrasser@yale.edu.

Funding

Function and Assembly of Eukaryotic ProteasomesR01GM083050 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 2008 to 2019
$3.8M
NIGMS NIH HHS GM083050NIGMS NIH HHS R01 GM083050Wellcome Trust 092076Wellcome Trust 103139Wellcome Trust 103139/Z/13/Z
6 · The paper itself

Abstract

Most short-lived eukaryotic proteins are degraded by the proteasome. A proteolytic core particle (CP) capped by regulatory particles (RPs) constitutes the 26S proteasome complex. RP biogenesis culminates with the joining of two large subcomplexes, the lid and base. In yeast and mammals, the lid appears to assemble completely before attaching to the base, but how this hierarchical assembly is enforced has remained unclear. Using biochemical reconstitutions, quantitative cross-linking/mass spectrometry, and electron microscopy, we resolve the mechanistic basis for the linkage between lid biogenesis and lid-base joining. Assimilation of the final lid subunit, Rpn12, triggers a large-scale conformational remodeling of the nascent lid that drives RP assembly, in part by relieving steric clash with the base. Surprisingly, this remodeling is triggered by a single Rpn12 α helix. Such assembly-coupled conformational switching is reminiscent of viral particle maturation and may represent a commonly used mechanism to enforce hierarchical assembly in multisubunit complexes.

Indexed as

Escherichia coliMass SpectrometryMicroscopy, ElectronModels, MolecularProteasome Endopeptidase ComplexProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATP dependent 26S proteaseProteasome Endopeptidase ComplexRPN12 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID26451487
PMCPMC4601081

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.