Evidence map›Paper›PMID 14517271›Full record

ArticleThe Journal of general physiology2003

Molecular coupling between voltage sensor and pore opening in the Arabidopsis inward rectifier K+ channel KAT1.

Ramon Latorre, Riccardo Olcese, Claudia Basso, Carlos Gonzalez, Fabian Munoz, Diego Cosmelli, Osvaldo Alvarez

Abstract read
In one paragraph

Article in The Journal of general physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Voltage sensors.Molecular pharmacology · 2025
    Review
  5. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  6. Article
  7. A folding reaction at the C-terminal domain drives temperature sensing in TRPM8 channels.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Bipolar switching by HCN voltage sensor underlies hyperpolarization activation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Review
  11. Gating control and KPlant, cell & environment · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  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

7 authors.

Ramon LatorreLaboratory of Biophysics and Molecular Physiology, Centro de Estudios Científicos, Valdivia, Chile. ramon@cecs.cl
Riccardo Olcese
Claudia Basso
Carlos Gonzalez
Fabian Munoz
Diego Cosmelli
Osvaldo Alvarez

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Animal and plant voltage-gated ion channels share a common architecture. They are made up of four subunits and the positive charges on helical S4 segments of the protein in animal K+ channels are the main voltage-sensing elements. The KAT1 channel cloned from Arabidopsis thaliana, despite its structural similarity to animal outward rectifier K+ channels is, however, an inward rectifier. Here we detected KAT1-gating currents due to the existence of an intrinsic voltage sensor in this channel. The measured gating currents evoked in response to hyperpolarizing voltage steps consist of a very fast (tau = 318 +/- 34 micros at -180 mV) and a slower component (4.5 +/- 0.5 ms at -180 mV) representing charge moved when most channels are closed. The observed gating currents precede in time the ionic currents and they are measurable at voltages (less than or equal to -60) at which the channel open probability is negligible ( approximately 10-4). These two observations, together with the fact that there is a delay in the onset of the ionic currents, indicate that gating charge transits between several closed states before the KAT1 channel opens. To gain insight into the molecular mechanisms that give rise to the gating currents and lead to channel opening, we probed external accessibility of S4 domain residues to methanethiosulfonate-ethyltrimethylammonium (MTSET) in both closed and open cysteine-substituted KAT1 channels. The results demonstrate that the putative voltage-sensing charges of S4 move inward when the KAT1 channels open.

Indexed as

Potassium Channels, Inwardly RectifyingAlgorithmsArabidopsisArabidopsis ProteinsDNA, ComplementaryElectrophysiologyIon Channel GatingMesylatesPatch-Clamp TechniquesPlant ProteinsPotassium ChannelsQuaternary Ammonium CompoundsRNA, MessengerArabidopsis ProteinsDNA, ComplementaryKAT1 protein, ArabidopsisMesylatesmethanethiosulfonatePlant ProteinsPotassium ChannelsPotassium Channels, Inwardly RectifyingQuaternary Ammonium CompoundsRNA, Messengertrimethylethylammonium

Identifiers

PMID14517271
PMCPMC2233774

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Registered trials

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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.