Evidence map›Paper›PMID 23755272›Full record

ArticlePloS one2013

Agp2, a member of the yeast amino acid permease family, positively regulates polyamine transport at the transcriptional level.

Mustapha Aouida, Marta Rubio-Texeira, Marta Rubio Texeira, Johan M Thevelein, Richard Poulin, Dindial Ramotar

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Optimized Combinations of Filtrates ofJournal of fungi (Basel, Switzerland) · 2025
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  8. Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. TheFrontiers in plant science · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Amino acid uptake in rust fungi.Frontiers in plant science · 2015
    Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Rubio Texeira, Marta [corrected to Rubio-Texeira, Marta]
5 · Who and what money

Authors and funding

6 authors at 4 institutions in 3 countries.

Mustapha AouidaCenter for Desert Agriculture, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia. Mustapha.aouida@kaust.edu.sa
Marta Rubio-Texeira
Marta Rubio Texeira
Johan M Thevelein
Richard Poulin
Dindial Ramotar
Vlaams Instituut voor Biotechnologie · BEHôpital Maisonneuve-Rosemont · CAKing Abdullah University of Science and Technology · SAUniversité Laval · CA

Funding

Canadian Institutes of Health Research MOP-67196Canadian Institutes of Health Research MOP-93573
6 · The paper itself

Abstract

Agp2 is a plasma membrane protein of the Saccharomyces cerevisiae amino acid transporter family, involved in high-affinity uptake of various substrates including L-carnitine and polyamines. The discovery of two high affinity polyamine permeases, Dur3 and Sam3, prompted us to investigate whether Agp2 directly transports polyamines or acts instead as a regulator. Herein, we show that neither dur3Δ nor sam3Δ single mutant is defective in polyamine transport, while the dur3Δ sam3Δ double mutant exhibits a sharp decrease in polyamine uptake and an increased resistance to polyamine toxicity similar to the agp2Δ mutant. Studies of Agp2 localization indicate that in the double mutant dur3Δ sam3Δ, Agp2-GFP remains plasma membrane-localized, even though transport of polyamines is strongly reduced. We further demonstrate that Agp2 controls the expression of several transporter genes including DUR3 and SAM3, the carnitine transporter HNM1 and several hexose, nucleoside and vitamin permease genes, in addition to SKY1 encoding a SR kinase that positively regulates low-affinity polyamine uptake. Furthermore, gene expression analysis clearly suggests that Agp2 is a strong positive regulator of additional biological processes. Collectively, our data suggest that Agp2 might respond to environmental cues and thus regulate the expression of several genes including those involved in polyamine transport.

Indexed as

Gene Expression Regulation, FungalTranscription, GeneticAmino Acid Transport SystemsBiological TransportCarnitineGene DeletionMembrane Transport ProteinsMolecular Sequence AnnotationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSpermidineSymportersAgp2 protein, S cerevisiaeAmino Acid Transport SystemsCarnitinecholine transporterDUR3 protein, S cerevisiaeMembrane Transport ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSAM3 protein, S cerevisiaeSKY1 protein, S cerevisiaeSpermidineSymporters

Identifiers

PMID23755272
PMCPMC3670898
OpenAlexW2080104294

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.