Evidence map›Paper›PMID 20739285›Full record

ArticleThe Journal of biological chemistry2010

Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12.

Christiane Riedinger, Jonas Boehringer, Jean-Francois Trempe, Edward D Lowe, Nicholas R Brown, Kalle Gehring, Martin E M Noble, Colin Gordon, Jane A Endicott

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 68 citations in OpenAlex.

  1. Characterization of the Regulatory AAA-ATPase Subunit Rpt3 inInternational journal of molecular sciences · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021
    Review
  10. Review
  11. Review
  12. Article
  13. Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018
    Review
  14. Article
  15. Proteasomes tether to two distinct sites at the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Structural basis for dynamic regulation of the human 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  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

9 authors at 3 institutions in 2 countries.

Christiane RiedingerLaboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
Jonas Boehringer
Jean-Francois Trempe
Edward D Lowe
Nicholas R Brown
Kalle Gehring
Martin E M Noble
Colin Gordon
Jane A Endicott
University of Oxford · GBMcGill University · CAWestern General Hospital · GB

Funding

CIHRMedical Research Council G0700053Medical Research Council MC_U127584486Wellcome Trust
6 · The paper itself

Abstract

Schizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19 S regulatory particle where it binds to subunits of both the base and lid subparticles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the von Willebrand factor type A domain and characterizing the full-length protein by NMR. We demonstrate that the single Ub-interacting motif (UIM) of SpRpn10 forms a 1:1 complex with Lys(48)-linked diUb, which it binds selectively over monoUb and Lys(63)-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid subparticle, with an affinity comparable with Lys(48)-linked diUb. This is the first observation of a UIM binding other than a Ub fold and suggests that SpRpn12 could modulate the activity of SpRpn10 as a proteasomal Ub receptor.

Indexed as

CalorimetryCarrier ProteinsHumansKineticsLysineMagnetic Resonance SpectroscopyPolyubiquitinProteasome Endopeptidase ComplexProtein BindingRNA-Binding ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSignal TransductionSurface Plasmon ResonanceUbiquitinvon Willebrand FactorCarrier ProteinsLysinePolyubiquitinProteasome Endopeptidase Complexpus1 protein, S pombeRNA-Binding ProteinsRPN12 protein, S pombeSchizosaccharomyces pombe ProteinsUbiquitinvon Willebrand Factor

Identifiers

PMID20739285
PMCPMC2962499
OpenAlexW2049226869

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.