Evidence map›Paper›PMID 12198087›Full record

ArticleThe Journal of general physiology2002

Coupling between voltage sensor activation, Ca2+ binding and channel opening in large conductance (BK) potassium channels.

Frank T Horrigan, Richard W Aldrich

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 346 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
346citing papers in PubMed, 1 pooled it
5.0field-weighted citation impact, top 4% 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

346 citing papers in PubMed, 1 synthesis or guideline pooled it, 512 citations in OpenAlex.

  1. Pooled it
  2. Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Potential therapeutic targeting of BKMolecular oncology · 2026
    Review
  7. Article
  8. The therapeutic pipeline in migraine: What does the future hold?Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2026
    Review
  9. Article
  10. Tuning the gate and the gear: The LRRC26 (γ1) subunit modulates intrinsic gating and voltage-sensor coupling of the BK channel.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. The BK channel-NS1619 agonist complex reveals molecular insights into allosteric activation gating.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  12. Article
  13. Review
  14. Article
  15. Tuning the gate and the gear: The LRRC26 (bioRxiv : the preprint server for biology · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Frank T HorriganDepartment of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. horrigan@mail.med.upenn.edu
Richard W Aldrich
Stanford University · USUniversity of Pennsylvania · US

Funding

Allosteric mechanisms of CA-activated K channel gatingR01NS042901 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI HORRIGAN, FRANK T · 2001 to 2011
$3.0M
SYNAPTIC TRANSMISSION AND PLASTICITY AT HIPPOCAMPAL SYNAPSESP50MH048108 · NIMH · STANFORD UNIVERSITY · PI TSIEN, RICHARD W · 1991 to 2000
$1.8M
NIMH NIH HHS MH48108NINDS NIH HHS NS42901NINDS NIH HHS R01 NS042901
6 · The paper itself

Abstract

To determine how intracellular Ca(2+) and membrane voltage regulate the gating of large conductance Ca(2+)-activated K(+) (BK) channels, we examined the steady-state and kinetic properties of mSlo1 ionic and gating currents in the presence and absence of Ca(2+) over a wide range of voltage. The activation of unliganded mSlo1 channels can be accounted for by allosteric coupling between voltage sensor activation and the closed (C) to open (O) conformational change (Horrigan, F.T., and R.W. Aldrich. 1999. J. Gen. Physiol. 114:305-336; Horrigan, F.T., J. Cui, and R.W. Aldrich. 1999. J. Gen. Physiol. 114:277-304). In 0 Ca(2+), the steady-state gating charge-voltage (Q(SS)-V) relationship is shallower and shifted to more negative voltages than the conductance-voltage (G(K)-V) relationship. Calcium alters the relationship between Q-V and G-V, shifting both to more negative voltages such that they almost superimpose in 70 microM Ca(2+). This change reflects a differential effect of Ca(2+) on voltage sensor activation and channel opening. Ca(2+) has only a small effect on the fast component of ON gating current, indicating that Ca(2+) binding has little effect on voltage sensor activation when channels are closed. In contrast, open probability measured at very negative voltages (less than -80 mV) increases more than 1,000-fold in 70 microM Ca(2+), demonstrating that Ca(2+) increases the C-O equilibrium constant under conditions where voltage sensors are not activated. Thus, Ca(2+) binding and voltage sensor activation act almost independently, to enhance channel opening. This dual-allosteric mechanism can reproduce the steady-state behavior of mSlo1 over a wide range of conditions, with the assumption that activation of individual Ca(2+) sensors or voltage sensors additively affect the energy of the C-O transition and that a weak interaction between Ca(2+) sensors and voltage sensors occurs independent of channel opening. By contrast, macroscopic I(K) kinetics indicate that Ca(2+) and voltage dependencies of C-O transition rates are complex, leading us to propose that the C-O conformational change may be described by a complex energy landscape.

Indexed as

Allosteric RegulationAnimalsCalciumFemaleHumansIon Channel GatingLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMiceOocytesPotassium ChannelsPotassium Channels, Calcium-ActivatedXenopusCalciumKcnma1 protein, mouseLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsPotassium ChannelsPotassium Channels, Calcium-Activated

Identifiers

PMID12198087
PMCPMC2229516
OpenAlexW2166084555

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.