Evidence map›Paper›PMID 27193484›Full record

ArticleScientific reports2016

Structural and functional insights into the E3 ligase, RNF126.

Ewelina M Krysztofinska, Santiago Martínez-Lumbreras, Arjun Thapaliya, Nicola J Evans, Stephen High, Rivka L Isaacson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. 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
1.9field-weighted citation impact, top 14% 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, 41 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Ewelina M KrysztofinskaDepartment of Chemistry, King's College London, Britannia House, Trinity Street, London, SE1 1DB, UK.
Santiago Martínez-LumbrerasDepartment of Chemistry, King's College London, Britannia House, Trinity Street, London, SE1 1DB, UK.
Arjun ThapaliyaDepartment of Chemistry, King's College London, Britannia House, Trinity Street, London, SE1 1DB, UK.
Nicola J EvansDepartment of Chemistry, King's College London, Britannia House, Trinity Street, London, SE1 1DB, UK.
Stephen HighFaculty of Life Sciences, University of Manchester, The Michael Smith Building, Oxford Road, Manchester, M13 9PT, UK.
Rivka L IsaacsonDepartment of Chemistry, King's College London, Britannia House, Trinity Street, London, SE1 1DB, UK.
King's College London · GBUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J014567/1Biotechnology and Biological Sciences Research Council BB/L006952/1Medical Research Council G0900936Wellcome TrustWellcome Trust 092107/Z/10/Z
6 · The paper itself

Abstract

RNF126 is an E3 ubiquitin ligase that collaborates with the BAG6 sortase complex to ubiquitinate hydrophobic substrates in the cytoplasm that are destined for proteasomal recycling. Composed of a trimeric complex of BAG6, TRC35 and UBL4A the BAG6 sortase is also associated with SGTA, a co-chaperone from which it can obtain hydrophobic substrates. Here we solve the solution structure of the RNF126 zinc finger domain in complex with the BAG6 UBL domain. We also characterise an interaction between RNF126 and UBL4A and analyse the competition between SGTA and RNF126 for the N-terminal BAG6 binding site. This work sheds light on the sorting mechanism of the BAG6 complex and its accessory proteins which, together, decide the fate of stray hydrophobic proteins in the aqueous cytoplasm.

Indexed as

Binding SitesCarrier ProteinsHeLa CellsHumansModels, MolecularMolecular ChaperonesMultiprotein ComplexesNuclear Magnetic Resonance, BiomolecularProtein BindingUbiquitin-Protein LigasesUbiquitinsZinc FingersBAG6 protein, humanCarrier ProteinsGET4 protein, humanMolecular ChaperonesMultiprotein ComplexesRNF126 protein, humanSGTA protein, humanUbiquitin-Protein LigasesUbiquitinsUbl4A protein, human

Identifiers

PMID27193484
PMCPMC4872217
OpenAlexW2404866411

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.