Evidence map›Paper›PMID 21765396›Full record

ArticleThe EMBO journal2011

Multiple modalities converge on a common gate to control K2P channel function.

Sviatoslav N Bagriantsev, Rémi Peyronnet, Kimberly A Clark, Eric Honoré, Daniel L Minor

Abstract 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. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing 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

104 citing papers in PubMed.

  1. Review
  2. Gating crosstalk in potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Modular architecture of KEMBO reports · 2025
    Review
  9. Structure of the human KNature structural & molecular biology · 2025
    Article
  10. 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
  11. The cryo-EM structure and physical basis for anesthetic inhibition of the THIK1 K2P channel.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Development of covalent chemogenetic KCell chemical biology · 2024
    Article
  17. Structure of the human KbioRxiv : the preprint server for biology · 2024
    Article
  18. Article
  19. Review
  20. Development of covalent chemogenetic KbioRxiv : the preprint server for biology · 2023
    Article

44 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

5 authors.

Sviatoslav N BagriantsevCardiovascular Research Institute, University of California, San Francisco, 94158-9001, USA.
Rémi Peyronnet
Kimberly A Clark
Eric Honoré
Daniel L Minor

Funding

Genetic and chemical biological studies of K2P structure, function, andmodulationR01MH093603 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DANIEL L MINOR · 2011 to 2026
$8.5M
Discovery and characterization of ion channel modulatorsR01NS049272 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MINOR, DANIEL L · 2004 to 2007
$1.4M
NIMH NIH HHS R01 MH093603NINDS NIH HHS R01 NS049272NINDS NIH HHS R01 NS49272
6 · The paper itself

Abstract

Members of the K(2P) potassium channel family regulate neuronal excitability and are implicated in pain, anaesthetic responses, thermosensation, neuroprotection, and mood. Unlike other potassium channels, K(2P)s are gated by remarkably diverse stimuli that include chemical, thermal, and mechanical modalities. It has remained unclear whether the various gating inputs act through separate or common channel elements. Here, we show that protons, heat, and pressure affect activity of the prototypical, polymodal K(2P), K(2P)2.1 (KCNK2/TREK-1), at a common molecular gate that comprises elements of the pore-forming segments and the N-terminal end of the M4 transmembrane segment. We further demonstrate that the M4 gating element is conserved among K(2P)s and is employed regardless of whether the gating stimuli are inhibitory or activating. Our results define a unique gating mechanism shared by K(2P) family members and suggest that their diverse sensory properties are achieved by coupling different molecular sensors to a conserved core gating apparatus.

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsHot TemperatureMiceMolecular Sequence DataPotassium Channels, Tandem Pore DomainPressureProtonspotassium channel protein TREK-1Potassium Channels, Tandem Pore DomainProtons

Identifiers

PMID21765396
PMCPMC3181481

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.