Evidence map›Paper›PMID 28814503›Full record

ArticleMolecular biology of the cell2017

Transition of yeast Can1 transporter to the inward-facing state unveils an α-arrestin target sequence promoting its ubiquitylation and endocytosis.

Christos Gournas, Elie Saliba, Eva-Maria Krammer, Céline Barthelemy, Martine Prévost, Bruno André

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 80 citations in OpenAlex.

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  11. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
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  20. Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020
    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

6 authors at 1 institution in 1 country.

Christos GournasMolecular Physiology of the Cell, Université Libre de Bruxelles, 6041 Gosselies, Belgium.
Elie SalibaMolecular Physiology of the Cell, Université Libre de Bruxelles, 6041 Gosselies, Belgium.
Eva-Maria KrammerStructure and Function of Biological Membranes, Université Libre de Bruxelles, 1050 Brussels, Belgium.
Céline BarthelemyMolecular Physiology of the Cell, Université Libre de Bruxelles, 6041 Gosselies, Belgium.
Martine PrévostStructure and Function of Biological Membranes, Université Libre de Bruxelles, 1050 Brussels, Belgium.
Bruno AndréMolecular Physiology of the Cell, Université Libre de Bruxelles, 6041 Gosselies, Belgium Bruno.Andre@ulb.ac.be.
Université Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Substrate-transport-elicited endocytosis is a common control mechanism of membrane transporters avoiding excess uptake of external compounds, though poorly understood at the molecular level. In yeast, endocytosis of transporters is triggered by their ubiquitylation mediated by the Rsp5 ubiquitin-ligase, recruited by α-arrestin-family adaptors. We here report that transport-elicited ubiquitylation of the arginine transporter Can1 is promoted by transition to an inward-facing state. This conformational change unveils a region of the N-terminal cytosolic tail targeted by the Art1 α-arrestin, which is activated via the TORC1 kinase complex upon arginine uptake. Can1 mutants altered in the arginine-binding site or a cytosolic tripeptide sequence permanently expose the α-arrestin-targeted region so that Art1 activation via TORC1 is sufficient to trigger their endocytosis. We also provide evidence that substrate-transport elicited endocytosis of other amino acid permeases similarly involves unmasking of a cytosolic Art1-target region coupled to activation of Art1 via TORC1. Our results unravel a mechanism likely involved in regulation of many other transporters by their own substrates. They also support the emerging view that transporter ubiquitylation relies on combinatorial interaction rules such that α-arrestins, stimulated via signaling cascades or in their basal state, recognize transporter regions permanently facing the cytosol or unveiled during transport.

Indexed as

Amino Acid Transport Systems, BasicArrestinBinding SitesCytosolEndocytosisEndosomal Sorting Complexes Required for TransportProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionStructure-Activity RelationshipTranscription FactorsUbiquitinUbiquitinationUbiquitin-Protein Ligase ComplexesAmino Acid Transport Systems, BasicArrestinCAN1 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUbiquitin-Protein Ligase Complexes

Identifiers

PMID28814503
PMCPMC5638585
OpenAlexW2747849226

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

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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.