Evidence map›Paper›PMID 16186565›Full record

ArticleThe Journal of general physiology2005

Gating and ionic currents reveal how the BKCa channel's Ca2+ sensitivity is enhanced by its beta1 subunit.

Lin Bao, Daniel H Cox

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

85 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mechanism of voltage sensing in CaProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021
    Review
  7. Review
  8. Review
  9. Calcium-Activated KHandbook of experimental pharmacology · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. The Journal of biological chemistry · 2019
    Article
  14. MitoBKThe Journal of physiology · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

25 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

2 authors at 1 institution in 1 country.

Lin BaoMolecular Cardiology Research Institute, New England Medical Center, Boston, MA 02111, USA.
Daniel H Cox
Tufts University · US

Funding

Regulation of BK Channel Gating by its Beta SubunitR01HL064831 · NHLBI · TUFTS UNIVERSITY BOSTON · PI COX, DANIEL HENRY · 2001 to 2010
$1.6M
NHLBI NIH HHS R01 HL064831NHLBI NIH HHS R01 HL 64831
6 · The paper itself

Abstract

Large-conductance Ca(2+)-activated K(+) channels (BK(Ca) channels) are regulated by the tissue-specific expression of auxiliary beta subunits. Beta1 is predominantly expressed in smooth muscle, where it greatly enhances the BK(Ca) channel's Ca(2+) sensitivity, an effect that is required for proper regulation of smooth muscle tone. Here, using gating current recordings, macroscopic ionic current recordings, and unitary ionic current recordings at very low open probabilities, we have investigated the mechanism that underlies this effect. Our results may be summarized as follows. The beta1 subunit has little or no effect on the equilibrium constant of the conformational change by which the BK(Ca) channel opens, and it does not affect the gating charge on the channel's voltage sensors, but it does stabilize voltage sensor activation, both when the channel is open and when it is closed, such that voltage sensor activation occurs at more negative voltages with beta1 present. Furthermore, beta1 stabilizes the active voltage sensor more when the channel is closed than when it is open, and this reduces the factor D by which voltage sensor activation promotes opening by approximately 24% (16.8-->12.8). The effects of beta1 on voltage sensing enhance the BK(Ca) channel's Ca(2+) sensitivity by decreasing at most voltages the work that Ca(2+) binding must do to open the channel. In addition, however, in order to fully account for the increase in efficacy and apparent Ca(2+) affinity brought about by beta1 at negative voltages, our studies suggest that beta1 also decreases the true Ca(2+) affinity of the closed channel, increasing its Ca(2+) dissociation constant from approximately 3.7 microM to between 4.7 and 7.1 microM, depending on how many binding sites are affected.

Indexed as

AnimalsBinding SitesCalciumCattleIon Channel GatingLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsMembrane PotentialsOocytesOsmolar ConcentrationPatch-Clamp TechniquesProtein ConformationTransfectionXenopus laevisCalciumLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta Subunits

Identifiers

PMID16186565
PMCPMC2266624
OpenAlexW2033433312

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.