Evidence map›Paper›PMID 32776922›Full record

ArticlePLoS genetics2020

Nitrogen coordinated import and export of arginine across the yeast vacuolar membrane.

Melody Cools, Simon Lissoir, Elisabeth Bodo, Judith Ulloa-Calzonzin, Alexander DeLuna, Isabelle Georis, Bruno André

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Age-based approach to characterize the dynamics of cellular processes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
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  8. Article
  9. Cellular quiescence in budding yeast.Yeast (Chichester, England) · 2021
    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

7 authors at 2 institutions in 2 countries.

Melody CoolsMolecular Physiology of the Cell, Université Libre de Bruxelles (ULB), Biopark, Gosselies, Belgium.ORCID 0000-0002-9933-0418
Simon LissoirMolecular Physiology of the Cell, Université Libre de Bruxelles (ULB), Biopark, Gosselies, Belgium.
Elisabeth BodoDéveloppement des bioprocédés et microbiologie appliquée, LABIRIS, Brussels, Belgium.
Judith Ulloa-CalzonzinUnidad de Genómica Avanzada (Langebio), Centro de Investigación y de Estudios Avanzados del IPN, Irapuato, Guanajuato, Mexico.
Alexander DeLunaUnidad de Genómica Avanzada (Langebio), Centro de Investigación y de Estudios Avanzados del IPN, Irapuato, Guanajuato, Mexico.ORCID 0000-0002-9236-2804
Isabelle GeorisMétabolisme des micro-organismes modèles, LABIRIS, Brussels, Belgium.ORCID 0000-0002-7763-5982
Bruno AndréMolecular Physiology of the Cell, Université Libre de Bruxelles (ULB), Biopark, Gosselies, Belgium.ORCID 0000-0002-4531-4674
Université Libre de Bruxelles · BEInstituto Politécnico Nacional · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The vacuole of the yeast Saccharomyces cerevisiae plays an important role in nutrient storage. Arginine, in particular, accumulates in the vacuole of nitrogen-replete cells and is mobilized to the cytosol under nitrogen starvation. The arginine import and export systems involved remain poorly characterized, however. Furthermore, how their activity is coordinated by nitrogen remains unknown. Here we characterize Vsb1 as a novel vacuolar membrane protein of the APC (amino acid-polyamine-organocation) transporter superfamily which, in nitrogen-replete cells, is essential to active uptake and storage of arginine into the vacuole. A shift to nitrogen starvation causes apparent inhibition of Vsb1-dependent activity and mobilization of stored vacuolar arginine to the cytosol. We further show that this arginine export involves Ypq2, a vacuolar protein homologous to the human lysosomal cationic amino acid exporter PQLC2 and whose activity is detected only in nitrogen-starved cells. Our study unravels the main arginine import and export systems of the yeast vacuole and suggests that they are inversely regulated by nitrogen.

Indexed as

Amino AcidsArginineBiological TransportHumansIntracellular MembranesLysosomesMembrane Transport ProteinsNitrogenSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesAmino AcidsArginineMembrane Transport ProteinsNitrogenSaccharomyces cerevisiae Proteins

Identifiers

PMID32776922
PMCPMC7440668
OpenAlexW3048679663

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.