Evidence map›Paper›PMID 24366945›Full record

ArticleThe EMBO journal2014

Dimeric Ube2g2 simultaneously engages donor and acceptor ubiquitins to form Lys48-linked ubiquitin chains.

Weixiao Liu, Yongliang Shang, Yan Zeng, Chao Liu, Yanchang Li, Linhui Zhai, Pan Wang, Jizhong Lou, Ping Xu, Yihong Ye and 1 more

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  7. Article
  8. Review
  9. Article
  10. Enzymatic Logic of Ubiquitin Chain Assembly.Frontiers in physiology · 2019
    Review
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  12. Article
  13. Article
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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

11 authors at 5 institutions in 2 countries.

Weixiao LiuState Key Laboratory of Reproductive Biology, Institute of Zoology Chinese Academy of Sciences, Beijing, China.
Yongliang Shang
Yan Zeng
Chao Liu
Yanchang Li
Linhui Zhai
Pan Wang
Jizhong Lou
Ping Xu
Yihong Ye
Wei Li
Chinese Academy of Sciences · CNBeijing Proteome Research Center · CNInstitute of Zoology · CNInstitute of Biophysics · CNNational Institutes of Health · US

Funding

Mechanism of protein retro-translocation from the endoplasmic reticulumZIADK033008 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YE, YIHONG · 2010 to 2025
$9.3M
Mechanism of polyubiquitin chain assembly by an ER-associated ubiquitin ligaseZIADK036137 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YE, YIHONG · 2009 to 2014
$486k
Intramural NIH HHS
6 · The paper itself

Abstract

Cellular adaptation to proteotoxic stress at the endoplasmic reticulum (ER) depends on Lys48-linked polyubiquitination by ER-associated ubiquitin ligases (E3s) and subsequent elimination of ubiquitinated retrotranslocation products by the proteasome. The ER-associated E3 gp78 ubiquitinates misfolded proteins by transferring preformed Lys48-linked ubiquitin chains from the cognate E2 Ube2g2 to substrates. Here we demonstrate that Ube2g2 synthesizes linkage specific ubiquitin chains by forming an unprecedented homodimer: The dimerization of Ube2g2, mediated primarily by electrostatic interactions between two Ube2g2s, is also facilitated by the charged ubiquitin molecules. Mutagenesis studies show that Ube2g2 dimerization is required for ER-associated degradation (ERAD). In addition to E2 dimerization, we show that a highly conserved arginine residue in the donor Ube2g2 senses the presence of an aspartate in the acceptor ubiquitin to position only Lys48 of ubiquitin in proximity to the donor E2 active site. These results reveal an unanticipated mode of E2 self-association that allows the E2 to effectively engage two ubiquitins to specifically synthesize Lys48-linked ubiquitin chains.

Indexed as

Protein MultimerizationAmino Acid SequenceCell LineDNA Mutational AnalysisHumansLysineModels, MolecularMolecular Sequence DataMutant ProteinsPolyubiquitinProtein BindingProtein ConformationUbiquitin-Conjugating EnzymesLysineMutant ProteinsPolyubiquitinUBE2G2 protein, humanUbiquitin-Conjugating Enzymes

Identifiers

PMID24366945
PMCPMC3990682
OpenAlexW2145096632

What OpenQuestion holds

Textmetadata
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.