Evidence map›Paper›PMID 26190103›Full record

ArticleCell reports2015

The Proteasome Distinguishes between Heterotypic and Homotypic Lysine-11-Linked Polyubiquitin Chains.

Guinevere L Grice, Ian T Lobb, Michael P Weekes, Steven P Gygi, Robin Antrobus, James A Nathan

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. MacrophageAutophagy · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Ubiquitination and Metabolic Disease.Advances in experimental medicine and biology · 2024
    Review
  9. Decoding Ubiquitin Modifications by Mass Spectrometry.Advances in experimental medicine and biology · 2024
    Review
  10. Review
  11. Review
  12. Atypical Ubiquitination and Parkinson's Disease.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021
    Review
  19. Review
  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

6 authors at 3 institutions in 2 countries.

Guinevere L GriceCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge Biomedical Research Centre, Cambridge CB2 0XY, UK.
Ian T LobbCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge Biomedical Research Centre, Cambridge CB2 0XY, UK.
Michael P WeekesCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge Biomedical Research Centre, Cambridge CB2 0XY, UK; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Robin AntrobusCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge Biomedical Research Centre, Cambridge CB2 0XY, UK.
James A NathanCambridge Institute for Medical Research, Department of Medicine, University of Cambridge, Cambridge Biomedical Research Centre, Cambridge CB2 0XY, UK. Electronic address: jan33@cam.ac.uk.
NIHR Cambridge Biomedical Research CentreHarvard University · USUniversity of Cambridge · GB

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
Medical Research Council G0802822NIGMS NIH HHS GM067945NIGMS NIH HHS R01 GM067945Wellcome Trust 093966/Z/10/ZWellcome Trust 100140Wellcome Trust 102770Wellcome Trust 102770/Z/13/Z
6 · The paper itself

Abstract

Proteasome-mediated degradation occurs with proteins principally modified with lysine-48 polyubiquitin chains. Whether the proteasome also can bind atypical ubiquitin chains, including those linked by lysine-11, has not been well established. This is critically important, as lysine-11 polyubiquitination has been implicated in both proteasome-mediated degradation and non-degradative outcomes. Here we demonstrate that pure homotypic lysine-11-linked chains do not bind strongly to the mammalian proteasome. By contrast, heterotypic polyubiquitin chains, containing lysine-11 and lysine-48 linkages, not only bind to the proteasome but also stimulate the proteasomal degradation of the cell-cycle regulator cyclin B1. Thus, while heterotypic lysine-11-linked chains facilitate proteasomal degradation, homotypic lysine-11 linkages adopt conformations that prevent association with the proteasome. Our data demonstrate the capacity of the proteasome to bind ubiquitin chains of distinct topology, with implications for the recognition and diverse biological functions of mixed ubiquitin chains.

Indexed as

UbiquitinationAmino Acid SequenceCyclin B1HeLa CellsHumansLysineMolecular Sequence DataPolyubiquitinProteasome Endopeptidase ComplexProtein BindingProteolysisSubstrate SpecificityCyclin B1LysinePolyubiquitinProteasome Endopeptidase Complex

Identifiers

PMID26190103
PMCPMC4533228
OpenAlexW1960421135

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.