Evidence map›Paper›PMID 28774922›Full record

ArticleScience (New York, N.Y.)2017

UBE2O is a quality control factor for orphans of multiprotein complexes.

Kota Yanagitani, Szymon Juszkiewicz, Ramanujan S Hegde

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

82 citing papers in PubMed, 136 citations in OpenAlex.

  1. Substrate biasing in UCHL5 proteoforms.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Structural evolution of the MTCH family of mitochondrial insertases.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Review
  8. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  9. Article
  10. Article
  11. Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. PEX1The Journal of biological chemistry · 2025
    Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

22 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Kota YanagitaniMedical Research Council (MRC) Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK.ORCID 0000-0002-5905-9950
Szymon JuszkiewiczMedical Research Council (MRC) Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK.ORCID 0000-0002-3361-7264
Ramanujan S HegdeMedical Research Council (MRC) Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK. rhegde@mrc-lmb.cam.ac.uk.ORCID 0000-0001-8338-852X
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_A022_1007
6 · The paper itself

Abstract

Many nascent proteins are assembled into multiprotein complexes of defined stoichiometry. Imbalances in the synthesis of individual subunits result in orphans. How orphans are selectively eliminated to maintain protein homeostasis is poorly understood. Here, we found that the conserved ubiquitin-conjugating enzyme UBE2O directly recognized juxtaposed basic and hydrophobic patches on unassembled proteins to mediate ubiquitination without a separate ubiquitin ligase. In reticulocytes, where UBE2O is highly up-regulated, unassembled α-globin molecules that failed to assemble with β-globin were selectively ubiquitinated by UBE2O. In nonreticulocytes, ribosomal proteins that did not engage nuclear import factors were targets for UBE2O. Thus, UBE2O is a self-contained quality control factor that comprises substrate recognition and ubiquitin transfer activities within a single protein to efficiently target orphans of multiprotein complexes for degradation.

Indexed as

ProteolysisUbiquitinationActive Transport, Cell Nucleusalpha-Globinsbeta-GlobinsCytosolHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsMultiprotein ComplexesReticulocytesRibosomal ProteinsSEC Translocation ChannelsUbiquitinUbiquitin-Conjugating Enzymesalpha-Globinsbeta-GlobinsMultiprotein ComplexesRibosomal ProteinsSEC61A1 protein, humanSEC Translocation ChannelsUBE2O protein, humanUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID28774922
PMCPMC5549844
OpenAlexW2744204310

What OpenQuestion holds

Textmetadata
LicenceTDM
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.