Evidence map›Paper›PMID 28716904›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Intracellular zinc activates KCNQ channels by reducing their dependence on phosphatidylinositol 4,5-bisphosphate.

Haixia Gao, Aurélien Boillat, Dongyang Huang, Ce Liang, Chris Peers, Nikita Gamper

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Caged ZnACS chemical neuroscience · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Chemical modulation of Kv7 potassium channels.RSC medicinal chemistry · 2021
    Review
  8. Review
  9. The role of labile ZnMolecular and cellular biochemistry · 2021
    Review
  10. Article
  11. Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021
    Article
  12. Insights into Potential Targets for Therapeutic Intervention in Epilepsy.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Kv7 Channels in Lung Diseases.Frontiers in physiology · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. M-type KBritish journal of pharmacology · 2018
    Review
  20. Impact of Labile Zinc on Heart Function: From Physiology to Pathophysiology.International journal of molecular sciences · 2017
    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

6 authors at 2 institutions in 2 countries.

Haixia GaoFaculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom.
Aurélien BoillatFaculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom.
Dongyang HuangDepartment of Pharmacology, Hebei Medical University, Shijiazhuang, China 050017.
Ce LiangDepartment of Pharmacology, Hebei Medical University, Shijiazhuang, China 050017.
Chris PeersLeeds Institute of Cardiovascular and Metabolic Medicine, Faculty of Medicine and Health, University of Leeds, Leeds LS2 9JT, United Kingdom.
Nikita GamperFaculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom; n.gamper@leeds.ac.uk.ORCID 0000-0001-5806-0207
Hebei Medical University · CNUniversity of Leeds · GB

Funding

Medical Research Council MR/K021303/1
6 · The paper itself

Abstract

M-type (Kv7, KCNQ) potassium channels are proteins that control the excitability of neurons and muscle cells. Many physiological and pathological mechanisms of excitation operate via the suppression of M channel activity or expression. Conversely, pharmacological augmentation of M channel activity is a recognized strategy for the treatment of hyperexcitability disorders such as pain and epilepsy. However, physiological mechanisms resulting in M channel potentiation are rare. Here we report that intracellular free zinc directly and reversibly augments the activity of recombinant and native M channels. This effect is mechanistically distinct from the known redox-dependent KCNQ channel potentiation. Interestingly, the effect of zinc cannot be attributed to a single histidine- or cysteine-containing zinc-binding site within KCNQ channels. Instead, zinc dramatically reduces KCNQ channel dependence on its obligatory physiological activator, phosphatidylinositol 4,5-bisphosphate (PIP

Indexed as

AnimalsBinding SitesCell LineCell MembraneCHO CellsCricetulusGanglia, SpinalHEK293 CellsHumansIon Channel GatingKCNQ Potassium ChannelsNeuronsOxidation-ReductionPatch-Clamp TechniquesPhosphatidylinositol 4,5-DiphosphateRatsKCNQ Potassium ChannelsPhosphatidylinositol 4,5-DiphosphateZincKCNQKv7M channelphosphatidylinositol 4,5-bisphosphatezinc

Identifiers

PMID28716904
PMCPMC5547594
OpenAlexW2735822849

What OpenQuestion holds

Textmetadata
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.