Evidence map›Paper›PMID 31015428›Full record

ArticleNature communications2019

Vps11 and Vps18 of Vps-C membrane traffic complexes are E3 ubiquitin ligases and fine-tune signalling.

Gregory Segala, Marcela A Bennesch, Nastaran Mohammadi Ghahhari, Deo Prakash Pandey, Pablo C Echeverria, François Karch, Robert K Maeda, Didier Picard

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.1field-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

26 citing papers in PubMed, 75 citations in OpenAlex.

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  14. Vps18 contributes to phagosome membrane integrity inbioRxiv : the preprint server for biology · 2023
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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

8 authors at 1 institution in 2 countries.

Gregory SegalaDépartement de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211, Genève, Switzerland.ORCID http://orcid.org/0000-0003-3533-0264
Marcela A BenneschDépartement de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211, Genève, Switzerland.
Nastaran Mohammadi GhahhariDépartement de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211, Genève, Switzerland.
Deo Prakash PandeyDépartement de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211, Genève, Switzerland.
Pablo C EcheverriaDépartement de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211, Genève, Switzerland.ORCID http://orcid.org/0000-0003-1367-9692
François KarchDépartement de Génétique et Évolution, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211, Genève, Switzerland.ORCID http://orcid.org/0000-0003-4722-5170
Robert K MaedaDépartement de Génétique et Évolution, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211, Genève, Switzerland.
Didier PicardDépartement de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211, Genève, Switzerland. didier.picard@unige.ch.ORCID http://orcid.org/0000-0001-8816-9668
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In response to extracellular signals, many signalling proteins associated with the plasma membrane are sorted into endosomes. This involves endosomal fusion, which depends on the complexes HOPS and CORVET. Whether and how their subunits themselves modulate signal transduction is unknown. We show that Vps11 and Vps18 (Vps11/18), two common subunits of the HOPS/CORVET complexes, are E3 ubiquitin ligases. Upon overexpression of Vps11/Vps18, we find perturbations of ubiquitination in signal transduction pathways. We specifically demonstrate that Vps11/18 regulate several signalling factors and pathways, including Wnt, estrogen receptor α (ERα), and NFκB. For ERα, we demonstrate that the Vps11/18-mediated ubiquitination of the scaffold protein PELP1 impairs the activation of ERα by c-Src. Thus, proteins involved in membrane traffic, in addition to performing their well-described role in endosomal fusion, fine-tune signalling in several different ways, including through ubiquitination.

Indexed as

Co-Repressor ProteinsCSK Tyrosine-Protein KinaseEndosomesEstrogen Receptor alphaHEK293 CellsHumansMCF-7 CellsNF-kappa BSignal Transductionsrc-Family KinasesTranscription FactorsUbiquitinationUbiquitin-Protein Ligase ComplexesVesicular Transport ProteinsWnt ProteinsCo-Repressor ProteinsCSK protein, humanCSK Tyrosine-Protein KinaseESR1 protein, humanEstrogen Receptor alphaNF-kappa BPELP1 protein, humansrc-Family KinasesTranscription FactorsUbiquitin-Protein Ligase ComplexesVesicular Transport ProteinsVPS11 protein, humanVPS18 protein, humanWnt Proteins

Identifiers

PMID31015428
PMCPMC6478910
OpenAlexW2941041091

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.