Evidence map›Paper›PMID 21724935›Full record

ArticleEukaryotic cell2011

A genomewide screen for tolerance to cationic drugs reveals genes important for potassium homeostasis in Saccharomyces cerevisiae.

Lina Barreto, David Canadell, Silvia Petrezsélyová, Clara Navarrete, Lydie Maresová, Jorge Peréz-Valle, Rito Herrera, Iván Olier, Jesús Giraldo, Hana Sychrová and 3 more

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2011. 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
2.3field-weighted citation impact, top 12% 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, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The KFrontiers in plant science · 2023
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  10. Yeast as a promising heterologous host for steroid bioproduction.Journal of industrial microbiology & biotechnology · 2020
    Review
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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

13 authors at 5 institutions in 2 countries.

Lina BarretoInstitut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Cerdanyola del Vallès 08193, Barcelona, Spain.
David Canadell
Silvia Petrezsélyová
Clara Navarrete
Lydie Maresová
Jorge Peréz-Valle
Rito Herrera
Iván Olier
Jesús Giraldo
Hana Sychrová
Lynne Yenush
José Ramos
Joaquín Ariño
Universitat Autònoma de Barcelona · ESCzech Academy of Sciences · CZUniversity of Córdoba · ESInstituto de Biología Molecular y Celular de Plantas · ESUniversitat Politècnica de València · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Potassium homeostasis is crucial for living cells. In the yeast Saccharomyces cerevisiae, the uptake of potassium is driven by the electrochemical gradient generated by the Pma1 H(+)-ATPase, and this process represents a major consumer of the gradient. We considered that any mutation resulting in an alteration of the electrochemical gradient could give rise to anomalous sensitivity to any cationic drug independently of its toxicity mechanism. Here, we describe a genomewide screen for mutants that present altered tolerance to hygromycin B, spermine, and tetramethylammonium. Two hundred twenty-six mutant strains displayed altered tolerance to all three drugs (202 hypersensitive and 24 hypertolerant), and more than 50% presented a strong or moderate growth defect at a limiting potassium concentration (1 mM). Functional groups such as protein kinases and phosphatases, intracellular trafficking, transcription, or cell cycle and DNA processing were enriched. Essentially, our screen has identified a substantial number of genes that were not previously described to play a direct or indirect role in potassium homeostasis. A subset of 27 representative mutants were selected and subjected to diverse biochemical tests that, in some cases, allowed us to postulate the basis for the observed phenotypes.

Indexed as

Biological TransportCation Transport ProteinsHomeostasisHygromycin BMembrane PotentialsMutationPhenotypePotassiumProton-Translocating ATPasesQuaternary Ammonium CompoundsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpermineCation Transport ProteinsHygromycin BPMA1 protein, S cerevisiaePotassiumProton-Translocating ATPasesQuaternary Ammonium CompoundsSaccharomyces cerevisiae ProteinsSperminetetramethylammoniumTRK1 protein, S cerevisiae

Identifiers

PMID21724935
PMCPMC3187046
OpenAlexW2119411909

What OpenQuestion holds

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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.