Evidence map›Paper›PMID 15111643›Full record

ArticleThe Journal of general physiology2004

Mapping the BKCa channel's "Ca2+ bowl": side-chains essential for Ca2+ sensing.

Lin Bao, Christina Kaldany, Ericka C Holmstrand, Daniel H Cox

Abstract read
In one paragraph

Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed.

  1. Article
  2. Review
  3. BK Channelopathies andAnnual review of physiology · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Coronary Large Conductance CaFrontiers in physiology · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Effects of Single Nucleotide Polymorphisms in HumanFrontiers in molecular neuroscience · 2019
    Article
  12. [Diltiazem inhibits proliferation and motility of hepatocellular cellsNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018
    Article
  13. Molecular determinants of CaScientific reports · 2018
    Article
  14. Review
  15. A voltage-dependent KThe Journal of cell biology · 2017
    Article
  16. Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017
    Review
  17. Article
  18. Review
  19. Store-Operated Calcium Channels.Physiological reviews · 2015
    Review
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Lin BaoMolecular Cardiology Research Institute, New England Medical Center, Department of Neuroscience, Tufts University School of Medicine, Boston, MA 02111, USA.
Christina Kaldany
Ericka C Holmstrand
Daniel H Cox

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 R01HL64831
6 · The paper itself

Abstract

There is controversy over whether Ca(2+) binds to the BK(Ca) channel's intracellular domain or its integral-membrane domain and over whether or not mutations that reduce the channel's Ca(2+) sensitivity act at the point of Ca(2+) coordination. One region in the intracellular domain that has been implicated in Ca(2+) sensing is the "Ca(2+) bowl". This region contains many acidic residues, and large Ca(2+)-bowl mutations eliminate Ca(2+) sensing through what appears to be one type of high-affinity Ca(2+)-binding site. Here, through site-directed mutagenesis we have mapped the residues in the Ca(2+) bowl that are most important for Ca(2+) sensing. We find acidic residues, D898 and D900, to be essential, and we find them essential as well for Ca(2+) binding to a fusion protein that contains a portion of the BK(Ca) channel's intracellular domain. Thus, much of our data supports the conclusion that Ca(2+) binds to the BK(Ca) channel's intracellular domain, and they define the Ca(2+) bowl's essential Ca(2+)-sensing motif. Overall, however, we have found that the relationship between mutations that disrupt Ca(2+) sensing and those that disrupt Ca(2+) binding is not as strong as we had expected, a result that raises the possibility that, when examined by gel-overlay, the Ca(2+) bowl may be in a nonnative conformation.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsCalciumCalcium SignalingCells, CulturedComputer SimulationIon Channel GatingLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMolecular Sequence DataMutagenesis, Site-DirectedMutationOocytesPotassium Channels, Calcium-ActivatedProtein BindingCalciumLarge-Conductance Calcium-Activated Potassium ChannelsPotassium Channels, Calcium-ActivatedRecombinant Proteins

Identifiers

PMID15111643
PMCPMC2234491

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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.