Evidence map›Paper›PMID 12034902›Full record

ArticleThe Plant cell2002

Physical and functional interaction of the Arabidopsis K(+) channel AKT2 and phosphatase AtPP2CA.

Isabelle Chérel, Erwan Michard, Nadine Platet, Karine Mouline, Carine Alcon, Hervé Sentenac, Jean-Baptiste Thibaud

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
11.8field-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

76 citing papers in PubMed, 199 citations in OpenAlex.

  1. A Salt-ResponsiveInternational journal of molecular sciences · 2026
    Article
  2. Review
  3. Structure reveals a regulation mechanism of plant outward-rectifying KProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Article
  6. Research Progress on Plant Shaker KPlants (Basel, Switzerland) · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Adjustment of KInternational journal of molecular sciences · 2021
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. International journal of molecular sciences · 2019
    Review
  19. Review
  20. Regulation of KFrontiers in plant science · 2019
    Review

16 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

7 authors at 2 institutions in 1 country.

Isabelle ChérelLaboratoire de Biochimie et Physiologie Moléculaire des Plantes, Unité Mixte de Recherche 5004 Agro-M/Centre National de la Recherche Scientifique/Institut National de la Recherche Agronomique/Université Montpellier II, France. cherel@ensam.inra.fr
Erwan Michard
Nadine Platet
Karine Mouline
Carine Alcon
Hervé Sentenac
Jean-Baptiste Thibaud
Institut des Sciences des Plantes de Montpellier · FRUniversité de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The AKT2 K(+) channel is endowed with unique functional properties, being the only weak inward rectifier characterized to date in Arabidopsis. The gene is expressed widely, mainly in the phloem but also at lower levels in leaf epiderm, mesophyll, and guard cells. The AKT2 mRNA level is upregulated by abscisic acid. By screening a two-hybrid cDNA library, we isolated a protein phosphatase 2C (AtPP2CA) involved in abscisic acid signaling as a putative partner of AKT2. We further confirmed the interaction by in vitro binding studies. The expression of AtPP2CA (beta-glucuronidase reporter gene) displayed a pattern largely overlapping that of AKT2 and was upregulated by abscisic acid. Coexpression of AtPP2CA with AKT2 in COS cells and Xenopus laevis oocytes was found to induce both an inhibition of the AKT2 current and an increase of the channel inward rectification. Site-directed mutagenesis and pharmacological analysis revealed that this functional interaction involves AtPP2CA phosphatase activity. Regulation of AKT2 activity by AtPP2CA in planta could allow the control of K(+) transport and membrane polarization during stress situations.

Indexed as

Arabidopsis ProteinsSaccharomyces cerevisiae ProteinsAbscisic AcidAnimalsArabidopsisCOS CellsDNA, ComplementaryGene Expression Regulation, EnzymologicGene Expression Regulation, PlantOocytesPhosphoprotein PhosphatasesPlant EpidermisPlant ProteinsPlant RootsPlant ShootsPotassium ChannelsAbscisic AcidAHG3 protein, ArabidopsisAKT2 protein, ArabidopsisArabidopsis ProteinsDNA, ComplementaryPhosphoprotein PhosphatasesPlant ProteinsPotassium ChannelsProtein Phosphatase 2Protein Phosphatase 2CPTC1 protein, S cerevisiaeRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID12034902
PMCPMC150612
OpenAlexW2145947875

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.