Evidence map›Paper›PMID 22733762›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Barium ions selectively activate BK channels via the Ca2+-bowl site.

Yu Zhou, Xu-Hui Zeng, Christopher J Lingle

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Astrocyte gap junctions and KFrontiers in cellular neuroscience · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. CaInternational journal of molecular sciences · 2023
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. FeACS chemical biology · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. A Role of BK Channel in Regulation of CaBiophysical journal · 2017
    Article
  19. Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017
    Review
  20. Interactions of divalent cations with calcium binding sites of BK channels reveal independent motions within the gating ring.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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

3 authors.

Yu ZhouDepartment of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Xu-Hui Zeng
Christopher J Lingle

Funding

Ion Channel Regulation by Ca2+R01GM066215 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2003 to 2015
$3.6M
AUXILIARY SUBUNITS OF CA2+ ACTIVATED K+ CHANNELSR01GM081748 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2008 to 2015
$3.2M
NIGMS NIH HHS GM-081748NIGMS NIH HHS R01 GM066215NIGMS NIH HHS R01 GM081748
6 · The paper itself

Abstract

Activation of Ca(2+)-dependent BK channels is increased via binding of micromolar Ca(2+) to two distinct high-affinity sites per BK α-subunit. One site, termed the Ca(2+) bowl, is embedded within the second RCK domain (RCK2; regulator of conductance for potassium) of each α-subunit, while oxygen-containing residues in the first RCK domain (RCK1) have been linked to a separate Ca(2+) ligation site. Although both sites are activated by Ca(2+) and Sr(2+), Cd(2+) selectively favors activation via the RCK1 site. Divalent cations of larger ionic radius than Sr(2+) are thought to be ineffective at activating BK channels. Here we show that Ba(2+), better known as a blocker of K(+) channels, activates BK channels and that this effect arises exclusively from binding at the Ca(2+)-bowl site. Compared with previous estimates for Ca(2+) bowl-mediated activation by Ca(2+), the affinity of Ba(2+) to the Ca(2+) bowl is reduced about fivefold, and coupling of binding to activation is reduced from ∼3.6 for Ca(2+) to about ∼2.8 for Ba(2+). These results support the idea that ionic radius is an important determinant of selectivity differences among different divalent cations observed for each Ca(2+)-binding site.

Indexed as

Allosteric SiteAnimalsBariumBinding SitesCalciumCationsElectrophysiologyHumansIonsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsModels, BiologicalModels, MolecularPotassium ChannelsStrontiumXenopus laevisBariumCalciumCationsIonsKCNMA1 protein, humanLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsPotassium ChannelsStrontium

Identifiers

PMID22733762
PMCPMC3396499

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.