Evidence map›Paper›PMID 23123110›Full record

ArticleStructure (London, England : 1993)2012

Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains.

Shan Liu, Yinghua Chen, Jess Li, Tao Huang, Sergey Tarasov, Aaren King, Allan M Weissman, R Andrew Byrd, Ranabir Das

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Exploring Sulfur Sites in Proteins via Triple-ResonanceJournal of the American Chemical Society · 2023
    Article
  2. Article
  3. Ubiquitination in the ERAD Process.International journal of molecular sciences · 2020
    Review
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  20. Cleaning up in the endoplasmic reticulum: ubiquitin in charge.Nature structural & molecular biology · 2014
    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

9 authors at 2 institutions in 1 country.

Shan LiuStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702-1201, USA.
Yinghua Chen
Jess Li
Tao Huang
Sergey Tarasov
Aaren King
Allan M Weissman
R Andrew Byrd
Ranabir Das
Center for Cancer Research · USNational Cancer Institute · US

Funding

Investigation of Protein-Protein Interactions in the ERAD Ubiquitylation PathwayZIABC011131 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2009 to 2024
$12.0M
CCR Biophysics Resource CoreZICBC010965 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI TARASOV, SERGEY · 2009 to 2025
$10.5M
Intramural NIH HHS ZIA BC011131
6 · The paper itself

Abstract

Recognition of ubiquitin and polyubiquitin chains by ubiquitin-binding domains (UBDs) is vital for ubiquitin-mediated signaling pathways. The endoplasmic reticulum resident RING finger ubiquitin ligase (E3) gp78 regulates critical proteins via the ubiquitin-proteasome system to maintain cellular homeostasis and includes a UBD known as the CUE domain, which is essential for function. A probable role of this domain is to recognize ubiquitin-modified substrates, enabling gp78 to assemble polyubiquitin chains on these substrates and mark them for degradation. Here, we report the molecular details of the interaction of gp78CUE domain with ubiquitin and diubiquitin. The gp78CUE domain exhibits a well-defined set of interactions with ubiquitin and a dynamic, promiscuous interaction with diubiquitin chains. This leads to a model in which the CUE domain functions to both facilitate substrate binding and enable switching between adjacent ubiquitin molecules of a growing chain to enable processivity in ubiquitination.

Indexed as

Amino Acid SequenceHumansHydrophobic and Hydrophilic InteractionsModels, MolecularNuclear Magnetic Resonance, BiomolecularPolyubiquitinProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryProtein Structure, SecondaryReceptors, Autocrine Motility FactorThermodynamicsAMFR protein, humanPolyubiquitinReceptors, Autocrine Motility Factor

Identifiers

PMID23123110
PMCPMC3518592
OpenAlexW2054919679

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.