Evidence map›Paper›PMID 21822218›Full record

ArticleThe EMBO journal2011

The pore structure and gating mechanism of K2P channels.

Paula L Piechotta, Markus Rapedius, Phillip J Stansfeld, Murali K Bollepalli, Gunter Ehrlich, Gunter Erhlich, Isabelle Andres-Enguix, Hariolf Fritzenschaft, Niels Decher, Mark S P Sansom and 2 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing 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

128 citing papers in PubMed, 156 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 2026
    Review
  5. Structure-Function Relationships of KAdvances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Structure of the human KNature structural & molecular biology · 2025
    Article
  8. 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
  9. Andrology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Development of covalent chemogenetic KCell chemical biology · 2024
    Article
  16. Structure of the human KbioRxiv : the preprint server for biology · 2024
    Article
  17. Article
  18. Article
  19. Two-pore potassium channel TREK-1 (K2P2.1) regulates NLRP3 inflammasome activity in macrophages.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  20. Differential contribution of THIK-1 KJournal of neuroinflammation · 2024
    Article

68 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
    Erhlich, Gunter [corrected to Ehrlich, Gunter]
5 · Who and what money

Authors and funding

12 authors at 4 institutions in 2 countries.

Paula L PiechottaUniversitätsklinikum Jena, Institute of Physiology II, Jena, Germany.
Markus Rapedius
Phillip J Stansfeld
Murali K Bollepalli
Gunter Ehrlich
Gunter Erhlich
Isabelle Andres-Enguix
Hariolf Fritzenschaft
Niels Decher
Mark S P Sansom
Stephen J Tucker
Thomas Baukrowitz
Kiel University · DEUniversity of Oxford · GBJena University Hospital · DEPhilipps University of Marburg · DE

Funding

Biotechnology and Biological Sciences Research Council B19456Biotechnology and Biological Sciences Research Council BB/H000267/1Biotechnology and Biological Sciences Research Council BB/I019855/1Biotechnology and Biological Sciences Research Council BBS/B/16011Biotechnology and Biological Sciences Research Council BEP17032Wellcome Trust 084655
6 · The paper itself

Abstract

Two-pore domain (K2P) potassium channels are important regulators of cellular electrical excitability. However, the structure of these channels and their gating mechanism, in particular the role of the bundle-crossing gate, are not well understood. Here, we report that quaternary ammonium (QA) ions bind with high-affinity deep within the pore of TREK-1 and have free access to their binding site before channel activation by intracellular pH or pressure. This demonstrates that, unlike most other K(+) channels, the bundle-crossing gate in this K2P channel is constitutively open. Furthermore, we used QA ions to probe the pore structure of TREK-1 by systematic scanning mutagenesis and comparison of these results with different possible structural models. This revealed that the TREK-1 pore most closely resembles the open-state structure of KvAP. We also found that mutations close to the selectivity filter and the nature of the permeant ion profoundly influence TREK-1 channel gating. These results demonstrate that the primary activation mechanisms in TREK-1 reside close to, or within the selectivity filter and do not involve gating at the cytoplasmic bundle crossing.

Indexed as

AnimalsBinding SitesHumansIon Channel GatingMutationPorosityPotassium Channel BlockersPotassium Channels, Tandem Pore DomainProtein ConformationQuaternary Ammonium CompoundsRatsPotassium Channel Blockerspotassium channel protein TREK-1Potassium Channels, Tandem Pore DomainQuaternary Ammonium Compounds

Identifiers

PMID21822218
PMCPMC3181484
OpenAlexW2079292159

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.