Evidence map›Paper›PMID 19794113›Full record

ArticleThe Plant cell2009

A tripartite SNARE-K+ channel complex mediates in channel-dependent K+ nutrition in Arabidopsis.

Annegret Honsbein, Sergei Sokolovski, Christopher Grefen, Prisca Campanoni, Réjane Pratelli, Manuel Paneque, Zhonghua Chen, Ingela Johansson, Michael R Blatt

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

78 citing papers in PubMed, 169 citations in OpenAlex.

  1. COJournal of integrative plant biology · 2026
    Article
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  7. Review
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  9. Analyzing Protein-Protein Interactions Using the Split-Ubiquitin System.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Review
  11. Engineering a KNature plants · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Identification and Characterization of Shaker KFrontiers in plant science · 2022
    Article
  16. Review
  17. The sorting of cargo proteins in the plantFrontiers in plant science · 2022
    Review
  18. Review
  19. Article
  20. ER-PM Contact Sites - SNARING Actors in Emerging Functions.Frontiers in cell and developmental biology · 2021
    Review

18 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

9 authors at 1 institution in 1 country.

Annegret HonsbeinFaculty of Biomedical and Life Sciences-Plant Sciences, University of Glasgow, Glasgow, United Kingdom.
Sergei Sokolovski
Christopher Grefen
Prisca Campanoni
Réjane Pratelli
Manuel Paneque
Zhonghua Chen
Ingela Johansson
Michael R Blatt
University of Glasgow · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D001528/1Biotechnology and Biological Sciences Research Council BB/F001630/1Biotechnology and Biological Sciences Research Council P12750
6 · The paper itself

Abstract

A few membrane vesicle trafficking (SNARE) proteins in plants are associated with signaling and transmembrane ion transport, including control of plasma membrane ion channels. Vesicle traffic contributes to the population of ion channels at the plasma membrane. Nonetheless, it is unclear whether these SNAREs also interact directly to affect channel gating and, if so, what functional impact this might have on the plant. Here, we report that the Arabidopsis thaliana SNARE SYP121 binds to KC1, a regulatory K(+) channel subunit that assembles with different inward-rectifying K(+) channels to affect their activities. We demonstrate that SYP121 interacts preferentially with KC1 over other Kv-like K(+) channel subunits and that KC1 interacts specifically with SYP121 but not with its closest structural and functional homolog SYP122 nor with another related SNARE SYP111. SYP121 promoted gating of the inward-rectifying K(+) channel AKT1 but only when heterologously coexpressed with KC1. Mutation in any one of the three genes, SYP121, KC1, and AKT1, selectively suppressed the inward-rectifying K(+) current in Arabidopsis root epidermal protoplasts as well as K(+) acquisition and growth in seedlings when channel-mediated K(+) uptake was limiting. That SYP121 should be important for gating of a K(+) channel and its role in inorganic mineral nutrition demonstrates an unexpected role for SNARE-ion channel interactions, apparently divorced from signaling and vesicle traffic. Instead, it suggests a role in regulating K(+) uptake coordinately with membrane expansion for cell growth.

Indexed as

AnimalsArabidopsisArabidopsis ProteinsElectrophysiologyGene Expression Regulation, PlantInsectaIon Channel GatingMutationOocytesPlant RootsPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingQa-SNARE ProteinsRNA, PlantXenopusAKT1 protein, ArabidopsisArabidopsis ProteinsPEN1 protein, ArabidopsisPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingQa-SNARE ProteinsRNA, Plant

Identifiers

PMID19794113
PMCPMC2768940
OpenAlexW2159515300

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.