Evidence map›Paper›PMID 19951915›Full record

ArticleThe Journal of cell biology2009

Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates.

Xiaoli Wang, Roger A Herr, Martijn Rabelink, Rob C Hoeben, Emmanuel J H J Wiertz, Ted H Hansen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

76 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Editorial: Reviews in ubiquitin signaling: 2022.Frontiers in molecular biosciences · 2023
    Article

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

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 2 institutions in 2 countries.

Xiaoli WangDepartment of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Roger A Herr
Martijn Rabelink
Rob C Hoeben
Emmanuel J H J Wiertz
Ted H Hansen
Leiden University Medical Center · NLWashington University in St. Louis · US

Funding

MHC-I regulation by herpes virusR01AI019687 · NIAID · WASHINGTON UNIVERSITY · PI FREMONT, DAVED H. · 1985 to 2016
$5.2M
NIAID NIH HHS AI019687NIAID NIH HHS R01 AI019687
6 · The paper itself

Abstract

Ubiquitin (Ub) modification of proteins plays a prominent role in the regulation of multiple cell processes, including endoplasmic reticulum-associated degradation (ERAD). Until recently, ubiquitination of substrates was thought to occur only via isopeptide bonds, typically to lysine residues. Several recent studies suggest that Ub can also be coupled to nonlysine residues by ester/thiolester bonds; however, the molecular basis for these novel modifications remains elusive. To probe the mechanism and importance of nonlysine ubiquitination, we have studied the viral ligase murine K3 (mK3), which facilitates the polyubiquitination of hydroxylated amino acids serine/threonine on its ERAD substrate. In this paper, we identify Ube2j2 as the primary cellular E2 recruited by the mK3 ligase, and this E2-E3 pair is capable of conjugating Ub on lysine or serine residues of substrates. However, surprisingly, Ube2j2-mK3 preferentially promotes ubiquitination of hydroxylated amino acids via ester bonds even when lysine residues are present on wild-type substrates, thus establishing physiological relevance of this novel ubiquitination strategy.

Indexed as

Amino Acid SequenceAnimalsCell LineEndoplasmic ReticulumIron-Binding ProteinsLigasesMajor Histocompatibility ComplexMiceMolecular Sequence DataProtein Structure, TertiarySequence AlignmentUbiquitinationUbiquitin-Conjugating EnzymesIron-Binding ProteinsLigasesUbe2d1 protein, mouseUBE2J2 protein, mouseUbiquitin-Conjugating Enzymes

Identifiers

PMID19951915
PMCPMC2806592
OpenAlexW1987428238

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.