Evidence map›Paper›PMID 20333436›Full record

ReviewCellular and molecular life sciences : CMLS2010

Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT transporter family.

C Corratgé-Faillie, M Jabnoune, S Zimmermann, A-A Véry, C Fizames, H Sentenac

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
19.0field-weighted citation impact, top 1% 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

109 citing papers in PubMed, 242 citations in OpenAlex.

  1. Salinity tolerance in wheat: rethinking the targets.Journal of experimental botany · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Regulation of potassium homeostasis inFrontiers in microbiology · 2026
    Article
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  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  14. Article
  15. Article
  16. c-di-AMP determines the hierarchical organization of bacterial RCK proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Inverse regulation of SOS1 and HKT1 protein localization and stability by SOS3/CBL4 inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  20. Article

49 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

6 authors at 4 institutions in 2 countries.

C Corratgé-FaillieBiochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier 2, 2 Place Viala, Montpellier Cedex 2, France.
M Jabnoune
S Zimmermann
A-A Véry
C Fizames
H Sentenac
Université de Montpellier · FRCentre National de la Recherche Scientifique · FRInstitut Agro Montpellier · FRInstitut des Sciences des Plantes de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial Trk and Ktr, fungal Trk and plant HKT form a family of membrane transporters permeable to K(+) and/or Na(+) and characterized by a common structure probably derived from an ancestral K(+) channel subunit. This transporter family, specific of non-animal cells, displays a large diversity in terms of ionic permeability, affinity and energetic coupling (H(+)-K(+) or Na(+)-K(+) symport, K(+) or Na(+) uniport), which might reflect a high need for adaptation in organisms living in fluctuating or dilute environments. Trk/Ktr/HKT transporters are involved in diverse functions, from K(+) or Na(+) uptake to membrane potential control, adaptation to osmotic or salt stress, or Na(+) recirculation from shoots to roots in plants. Structural analyses of bacterial Ktr point to multimeric structures physically interacting with regulatory subunits. Elucidation of Trk/Ktr/HKT protein structures along with characterization of mutated transporters could highlight functional and evolutionary relationships between ion channels and transporters displaying channel-like features.

Indexed as

Biological TransportIon ChannelsIon TransportMembrane PotentialsMembrane Transport ProteinsMutationPlant RootsPlantsPotassiumSodiumSodium, DietaryIon ChannelsMembrane Transport ProteinsPotassiumSodiumSodium, Dietary

Identifiers

PMID20333436
PMCPMC11115768
OpenAlexW2050839170

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.