Evidence map›Paper›PMID 29559531›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Conformation-dependent partitioning of yeast nutrient transporters into starvation-protective membrane domains.

Christos Gournas, Stelios Gkionis, Mélanie Carquin, Laure Twyffels, Donatienne Tyteca, Bruno André

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.1field-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

40 citing papers in PubMed, 78 citations in OpenAlex.

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  18. 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 3 institutions in 1 country.

Christos GournasMolecular Physiology of the Cell, Institut de Biologie et de Médecine Moléculaires, Université Libre de Bruxelles, 6041 Gosselies, Belgium; Christos.Gournas@ulb.ac.be Bruno.Andre@ulb.ac.be.
Stelios GkionisMolecular Physiology of the Cell, Institut de Biologie et de Médecine Moléculaires, Université Libre de Bruxelles, 6041 Gosselies, Belgium.
Mélanie CarquinBiologie Cellulaire, de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium.
Laure TwyffelsCenter for Microscopy and Molecular Imaging, Université Libre de Bruxelles, 6041 Gosselies, Belgium.
Donatienne TytecaBiologie Cellulaire, de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium.
Bruno AndréMolecular Physiology of the Cell, Institut de Biologie et de Médecine Moléculaires, Université Libre de Bruxelles, 6041 Gosselies, Belgium; Christos.Gournas@ulb.ac.be Bruno.Andre@ulb.ac.be.
Université Libre de Bruxelles · BEde Duve Institute · BEUCLouvain · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The eukaryotic plasma membrane is compartmentalized into domains enriched in specific lipids and proteins. However, our understanding of the molecular bases and biological roles of this partitioning remains incomplete. The best-studied domain in yeast is the membrane compartment containing the arginine permease Can1 (MCC) and later found to cluster additional transporters. MCCs correspond to static, furrow-like invaginations of the plasma membrane and associate with subcortical structures named "eisosomes" that include upstream regulators of the target of rapamycin complex 2 (TORC2) in the sensing of sphingolipids and membrane stress. However, how and why Can1 and other nutrient transporters preferentially segregate in MCCs remains unknown. In this study we report that the clustering of Can1 in MCCs is dictated by its conformation, requires proper sphingolipid biosynthesis, and controls its ubiquitin-dependent endocytosis. In the substrate-free outward-open conformation, Can1 accumulates in MCCs in a manner dependent on sustained biogenesis of complex sphingolipids. An arginine transport-elicited shift to an inward-facing conformation promotes its cell-surface dissipation and makes it accessible to the ubiquitylation machinery triggering its endocytosis. We further show that under starvation conditions MCCs increase in number and size, this being dependent on the BAR domain-containing Lsp1 eisosome component. This expansion of MCCs provides protection for nutrient transporters from bulk endocytosis occurring in parallel with autophagy upon TORC1 inhibition. Our study reveals nutrient-regulated protection from endocytosis as an important role for protein partitioning into membrane domains.

Indexed as

FoodStarvationAmino Acid Transport Systems, BasicCell MembraneEndocytosisMechanistic Target of Rapamycin Complex 1Molecular ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSphingolipidsUbiquitinationAmino Acid Transport Systems, BasicCAN1 protein, S cerevisiaeMechanistic Target of Rapamycin Complex 1Saccharomyces cerevisiae ProteinsSphingolipidsendocytosismembrane domaintransporterubiquitinyeast

Identifiers

PMID29559531
PMCPMC5889650
OpenAlexW2794194614

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.