Evidence map›Paper›PMID 27678051›Full record

ArticleJournal of molecular biology2016

Role of E2-RING Interactions in Governing RNF4-Mediated Substrate Ubiquitination.

Anthony DiBello, Ajit B Datta, Xiangbin Zhang, Cynthia Wolberger

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. The role of ubiquitin-conjugating enzyme in the process of spermatogenesis.Reproductive biology and endocrinology : RB&E · 2024
    Review
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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

4 authors at 1 institution in 1 country.

Anthony DiBelloDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
Ajit B DattaDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
Xiangbin ZhangDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
Cynthia WolbergerDepartment of Biophysics and Biophysical Chemistry, The Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA. Electronic address: cwolberg@jhmi.edu.
Johns Hopkins University · US

Funding

REGULATION OF UBIQUITINATION BY DUB-E2 UBIQUITIN CONJUGATING ENZYME COMPLEXESR01GM109102 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOLBERGER, CYNTHIA · 2014 to 2017
$1.9M
NIGMS NIH HHS R01 GM109102
6 · The paper itself

Abstract

Members of the really interesting new gene (RING) E3 ubiquitin ligase family bind to both substrate and ubiquitin-charged E2 enzyme, promoting the transfer of ubiquitin from the E2 to substrate. Either a single ubiquitin or one of the several types of polyubiquitin chains can be conjugated to substrate proteins, with different types of ubiquitin modifications signaling the distinct outcomes. E2 enzymes play a central role in governing the nature of the ubiquitin modification, although the essential features of the E2 that differentiate mono- versus polyubiquitinating E2 enzymes remain unclear. RNF4 is a compact RING E3 ligase that directs the ubiquitination of polySUMO chains in concert with several different E2 enzymes. RNF4 monoubiquitinates polySUMO substrates in concert with RAD6B and polyubiquitinates substrates together with UBCH5B, a promiscuous E2 that can function with a broad range of E3 ligases. We find that the divergent ubiquitination activities of RAD6B and UBCH5B are governed by differences at the RING-binding surface of the E2. By mutating the RAD6B RING-binding surface to resemble that of UBCH5B, RAD6B can be transformed into a highly active UBCH5B-like E2 that polyubiquitinates SUMO chains in concert with RNF4. The switch in RAD6B activity correlates with increased affinity of the E2 for RNF4. These results point to an important role of the affinity between an E3 and its cognate E2 in governing the multiplicity of substrate ubiquitination.

Indexed as

Protein Processing, Post-TranslationalUbiquitinationHumansNuclear ProteinsSmall Ubiquitin-Related Modifier ProteinsTranscription FactorsUbiquitin-Conjugating EnzymesNuclear ProteinsRNF4 protein, humanSmall Ubiquitin-Related Modifier ProteinsTranscription FactorsUBE2B protein, humanUBE2D2 protein, humanUbiquitin-Conjugating EnzymesE2 ubiquitin-conjugating enzymeE3 ubiquitin ligaseRAD6BRING finger protein 4 (RNF4)ubiquitin

Identifiers

PMID27678051
PMCPMC5115946
OpenAlexW2523184587

What OpenQuestion holds

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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.