Evidence map›Paper›PMID 24517091›Full record

ArticleThe Plant journal : for cell and molecular biology2014

Clustering of the K+ channel GORK of Arabidopsis parallels its gating by extracellular K+.

Cornelia Eisenach, Maria Papanatsiou, Ellin-Kristina Hillert, Michael R Blatt

Open access · hybridAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
7.5field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. COJournal of integrative plant biology · 2026
    Article
  3. Article
  4. GORK KNature communications · 2025
    Article
  5. Article
  6. Identification and Characterization ofInternational journal of molecular sciences · 2024
    Article
  7. Article
  8. Review
  9. Speedy stomata of a CPlant, cell & environment · 2024
    Article
  10. Article
  11. Article
  12. Engineering a KNature plants · 2022
    Article
  13. Article
  14. Review
  15. Lipid kinases PIP5K7 and PIP5K9 are required for polyamine-triggered KThe Plant journal : for cell and molecular biology · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Cornelia EisenachLaboratory of Plant Physiology and Biophysics, Institute of Molecular, Cell and Systems Biology, University of Glasgow, Bower Building, Glasgow, G12 8QQ, UK.
Maria Papanatsiou
Ellin-Kristina Hillert
Michael R Blatt
University of Glasgow · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C500595/1Biotechnology and Biological Sciences Research Council BB/F001630/1Biotechnology and Biological Sciences Research Council BB/F001673/1Biotechnology and Biological Sciences Research Council BB/H009817/1Biotechnology and Biological Sciences Research Council BB/I024496/1Biotechnology and Biological Sciences Research Council P12750
6 · The paper itself

Abstract

GORK is the only outward-rectifying Kv-like K(+) channel expressed in guard cells. Its activity is tightly regulated to facilitate K(+) efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward-rectifying K(+) channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently-tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K(+) concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K(+) channel blocker Ba(2+) . By contrast, confocal and protein biochemical analysis failed to uncover substantial exo- and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K(+) , a characteristic that ensures the channel facilitates only K(+) efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K(+) above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K(+) .

Indexed as

ArabidopsisArabidopsis ProteinsBiological TransportPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingPotassium ChlorideArabidopsis ProteinsGORK protein, ArabidopsisKAT1 protein, ArabidopsisPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingPotassium ChlorideArabidopsischannel gating - K+-dependentconfocal microscopyGORK K+ channel - outward-rectifyingK+ concentration - extracellularmembrane vesicle trafficplasma membrane

Identifiers

PMID24517091
PMCPMC4309415
OpenAlexW2138192759

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.