Evidence map›Paper›PMID 21757998›Full record

ArticlePlant signaling & behavior2011

Membrane localisation diversity of TPK channels and their physiological role.

Stanislav Isayenkov, Jean-Charles Isner, Frans J M Maathuis

Open access · bronzeAbstract read
In one paragraph

Article in Plant signaling & behavior, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

11 citing papers in PubMed, 32 citations in OpenAlex.

  1. A genome-wide association analysis identifies a key candidate gene controlling plant growth habit in chickpea.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
    Article
  2. Review
  3. Functional genomic analysis of KFrontiers in plant science · 2022
    Article
  4. New Insights into Plant TPK Ion Channel Evolution.Plants (Basel, Switzerland) · 2021
    Article
  5. Article
  6. Article
  7. HFrontiers in plant science · 2018
    Article
  8. Article
  9. K₂p channels in plants and animals.Pflugers Archiv : European journal of physiology · 2015
    Review
  10. Article
  11. Article
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

3 authors at 2 institutions in 3 countries.

Stanislav IsayenkovDepartment of Genomics and Molecular Biotechnology, Institute of Food Biotechnology and Genomics, Kiev, Ukraine.
Jean-Charles Isner
Frans J M Maathuis
University of York · GBInstitute of Food Biotechnology and Genomics · UA

Funding

Biotechnology and Biological Sciences Research Council BB/C510032/1Biotechnology and Biological Sciences Research Council BB/E527155/1
6 · The paper itself

Abstract

Potassium (K) is one of the major nutrients that is essential for plant growth and development. The majority of cellular K+ resides in the vacuole and tonoplast K+ channels of the TPK (Two Pore K) family are main players in cellular K+ homeostasis. All TPK channels were previously reported to be expressed in the tonoplast of the large central lytic vacuole (LV) except for one isoform in Arabidopsis that resides in the plasma membrane. However, plant cells often contain more than one type of vacuole that coexist in the same cell. We recently showed that two TPK isoforms (OsTPKa and OsTPKb) from Oryza sativa localise to different vacuoles with OsTPKa predominantly found in the LV tonoplast and OsTPKb primarily in smaller compartments that resemble small vacuoles (SVs). Our study further revealed that it is the C-terminal domain that determines differential targeting of OsTPKa and OsTPKb. Three C-terminal amino acids were particularly relevant for targeting TPKs to their respective endomembranes. In this addendum we further evaluate how the different localisation of TPKa and TPKb impact on their physiological role and how TPKs provide a potential tool to study the physiology of different types of vacuole.

Indexed as

OryzaPlant ProteinsPotassiumPotassium Channels, Tandem Pore DomainProtein IsoformsProtein Structure, SecondaryVacuolesPlant ProteinsPotassiumPotassium Channels, Tandem Pore DomainProtein Isoforms

Identifiers

PMID21757998
PMCPMC3260722
OpenAlexW1964839656

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.