Evidence map›Paper›PMID 11867520›Full record

ArticleThe EMBO journal2002

The Ppz protein phosphatases are key regulators of K+ and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression.

Lynne Yenush, José M Mulet, Joaquín Ariño, Ramón Serrano

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
11.3field-weighted citation impact, top 2% 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

66 citing papers in PubMed, 138 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Journal of fungi (Basel, Switzerland) · 2022
    Article
  5. Article
  6. Fungal Hal3 (and Its Close Relative Cab3) as Moonlighting Proteins.Journal of fungi (Basel, Switzerland) · 2022
    Review
  7. Article
  8. When Phosphatases Go Mad: The Molecular Basis for Toxicity of Yeast Ppz1.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. International journal of molecular sciences · 2019
    Review
  17. Review
  18. Article
  19. Evolutionary engineering inBiotechnology for biofuels · 2019
    Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Lynne YenushInstituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-CSIC, Camino de Vera s/n, E-46022 Valencia, Spain. serrano@ibmcp.upv.es
José M Mulet
Joaquín Ariño
Ramón Serrano
Instituto de Biología Molecular y Celular de Plantas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast Ppz protein phosphatases and the Hal3p inhibitory subunit are important determinants of salt tolerance, cell wall integrity and cell cycle progression. We present several lines of evidence showing that these disparate phenotypes are connected by the fact that Ppz regulates K+ transport. First, salt tolerance, cell wall integrity and cell cycle phenotypes of Ppz mutants are dependent on the Trk K+ transporters. Secondly, Ppz mutants exhibit altered activity of the Trk system, as measured by rubidium uptake. Thirdly, Ppz mutants exhibit altered intracellular K+ and pH, as expected from H+ efflux providing electrical balance during K+ uptake. Our unifying picture of Ppz phenotypes contends that activation of Trk by decreased Ppz activity results in plasma membrane depolarization (reducing uptake of toxic cations), increased intracellular K+ and turgor (compromising cell integrity), and increased intracellular pH (augmenting the expression of pH-regulated genes and facilitating alpha-factor recovery). In addition to providing a coherent explanation for all Ppz-dependent phenotypes, our results provide evidence for a causal relationship between intracellular cation homeostasis and a potential cell cycle checkpoint.

Indexed as

Cation Transport ProteinsCell Cycle ProteinsFungal ProteinsAdenosine TriphosphatasesCarrier ProteinsCell CycleCell WallG1 PhaseHomeostasisIon TransportMating FactorMembrane ProteinsOsmotic FragilityPeptidesPhenotypePhosphoprotein PhosphatasesAdenosine TriphosphatasesCarrier ProteinsCation Transport ProteinsCell Cycle ProteinsENA1 protein, S cerevisiaeFungal ProteinsMating FactorMembrane ProteinsPeptidesPhosphoprotein PhosphatasesPMA1 protein, S cerevisiaePotassiumPotassium ChloridePPZ1 protein, S cerevisiaePPZ2 protein, S cerevisiaeProton-Translocating ATPasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSIS2 protein, S cerevisiaeSodium-Potassium-Exchanging ATPaseTRK1 protein, S cerevisiaeTRK2 protein, S cerevisiae

Identifiers

PMID11867520
PMCPMC125902
OpenAlexW2079158026

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.