Evidence map›Paper›PMID 26919430›Full record

ArticleCell2016

A Non-canonical Voltage-Sensing Mechanism Controls Gating in K2P K(+) Channels.

Marcus Schewe, Ehsan Nematian-Ardestani, Han Sun, Marianne Musinszki, Sönke Cordeiro, Giovanna Bucci, Bert L de Groot, Stephen J Tucker, Markus Rapedius, Thomas Baukrowitz

Abstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing 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

134 citing papers in PubMed.

  1. Similarity of the ion occupations of KChannels (Austin, Tex.) · 2026
    Article
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  5. Review
  6. Article
  7. Article
  8. The diabetes-associated KDiabetologia · 2026
    Article
  9. Article
  10. Article
  11. Structure-Function Relationships of KAdvances in experimental medicine and biology · 2026
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Modular architecture of KEMBO reports · 2025
    Review
  17. Article
  18. Structure of the human KNature structural & molecular biology · 2025
    Article
  19. Structure of the human TWIK-2 potassium channel and its inhibition by pimozide.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Roles of PDGF/PDGFR signaling in various organs.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2025
    Review

74 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

10 authors.

Marcus ScheweInstitute of Physiology, Christian-Albrechts University, 24118 Kiel, Germany.
Ehsan Nematian-ArdestaniInstitute of Physiology, Christian-Albrechts University, 24118 Kiel, Germany.
Han SunComputational Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany; Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany.
Marianne MusinszkiInstitute of Physiology, Christian-Albrechts University, 24118 Kiel, Germany.
Sönke CordeiroInstitute of Physiology, Christian-Albrechts University, 24118 Kiel, Germany.
Giovanna BucciClarendon Laboratory, Department of Physics, University of Oxford, Oxford OX1 3PU, UK.
Bert L de GrootComputational Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Stephen J TuckerClarendon Laboratory, Department of Physics, University of Oxford, Oxford OX1 3PU, UK; OXION Initiative, University of Oxford, Oxford OX1 3PU, UK.
Markus RapediusInstitute of Physiology, Christian-Albrechts University, 24118 Kiel, Germany; Nanion Technologies GmbH, 80636 Munich, Germany.
Thomas BaukrowitzInstitute of Physiology, Christian-Albrechts University, 24118 Kiel, Germany. Electronic address: t.baukrowitz@physiologie.uni-kiel.de.

Funding

Biotechnology and Biological Sciences Research CouncilBritish Heart Foundation PG/09/016/26992Wellcome Trust
6 · The paper itself

Abstract

Two-pore domain (K2P) K(+) channels are major regulators of excitability that endow cells with an outwardly rectifying background "leak" conductance. In some K2P channels, strong voltage-dependent activation has been observed, but the mechanism remains unresolved because they lack a canonical voltage-sensing domain. Here, we show voltage-dependent gating is common to most K2P channels and that this voltage sensitivity originates from the movement of three to four ions into the high electric field of an inactive selectivity filter. Overall, this ion-flux gating mechanism generates a one-way "check valve" within the filter because outward movement of K(+) induces filter opening, whereas inward movement promotes inactivation. Furthermore, many physiological stimuli switch off this flux gating mode to convert K2P channels into a leak conductance. These findings provide insight into the functional plasticity of a K(+)-selective filter and also refine our understanding of K2P channels and the mechanisms by which ion channels can sense voltage.

Indexed as

ElectrophysiologyHumansKineticsMolecular Dynamics SimulationPotassiumPotassium Channels, Tandem Pore DomainPotassiumPotassium Channels, Tandem Pore Domain

Identifiers

PMID26919430
PMCPMC4771873

What OpenQuestion holds

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LicenceCC BY
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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.