Evidence map›Paper›PMID 23942235›Full record

ArticleThe EMBO journal2013

Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine.

Ranabir Das, Yu-He Liang, Jennifer Mariano, Jess Li, Tao Huang, Aaren King, Sergey G Tarasov, Allan M Weissman, Xinhua Ji, R Andrew Byrd

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Article
  3. Internal Ubiquitin Electrophiles for Covalent Trapping and Inhibition of Deubiquitinases.Chembiochem : a European journal of chemical biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Targeting TRIM Proteins: A Quest towards Drugging an Emerging Protein Class.Chembiochem : a European journal of chemical biology · 2021
    Review
  18. Article
  19. Review
  20. Article

3 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

10 authors at 3 institutions in 1 country.

Ranabir DasStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, USA.
Yu-He Liang
Jennifer Mariano
Jess Li
Tao Huang
Aaren King
Sergey G Tarasov
Allan M Weissman
Xinhua Ji
R Andrew Byrd
Center for Cancer Research · USNational Cancer Institute · USFrederick National Laboratory for Cancer Research · US

Funding

Biomolecular Structure and Mechanism, Structure-Based Drug DesignZIABC010326 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI JI, XINHUA · 2009 to 2024
$27.3M
Enzymes and Substrates of the Ubiquitin Conjugating SystemZIABC010292 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WEISSMAN, ALLAN M · 2009 to 2024
$12.2M
Investigation of Protein-Protein Interactions in the ERAD Ubiquitylation PathwayZIABC011131 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2009 to 2024
$12.0M
Intramural NIH HHS
6 · The paper itself

Abstract

RING finger proteins constitute the large majority of ubiquitin ligases (E3s) and function by interacting with ubiquitin-conjugating enzymes (E2s) charged with ubiquitin. How low-affinity RING-E2 interactions result in highly processive substrate ubiquitination is largely unknown. The RING E3, gp78, represents an excellent model to study this process. gp78 includes a high-affinity secondary binding region for its cognate E2, Ube2g2, the G2BR. The G2BR allosterically enhances RING:Ube2g2 binding and ubiquitination. Structural analysis of the RING:Ube2g2:G2BR complex reveals that a G2BR-induced conformational effect at the RING:Ube2g2 interface is necessary for enhanced binding of RING to Ube2g2 or Ube2g2 conjugated to Ub. This conformational effect and a key ternary interaction with conjugated ubiquitin are required for ubiquitin transfer. Moreover, RING:Ube2g2 binding induces a second allosteric effect, disrupting Ube2g2:G2BR contacts, decreasing affinity and facilitating E2 exchange. Thus, gp78 is a ubiquitination machine where multiple E2-binding sites coordinately facilitate processive ubiquitination.

Indexed as

Models, MolecularProtein ConformationAllosteric RegulationAmino Acid SequenceCloning, MolecularCrystallography, X-RayEscherichia coliHumansMagnetic Resonance SpectroscopyMolecular Sequence DataMultiprotein ComplexesProtein BindingReceptors, Autocrine Motility FactorUbiquitinationUbiquitin-Conjugating EnzymesAMFR protein, humanMultiprotein ComplexesReceptors, Autocrine Motility FactorUBE2G2 protein, humanUbiquitin-Conjugating Enzymes

Identifiers

PMID23942235
PMCPMC3770950
OpenAlexW2148702226

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.