ArticleThe Journal of general physiology1997
Allosteric gating of a large conductance Ca-activated K+ channel.
Article in The Journal of general physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 173 papers.
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Who cites it
173 citing papers in PubMed, 260 citations in OpenAlex.
- Evolution towards higher unitary conductance in mammals makes BK channels more efficient and precise.Communications biology · 2026Article
- 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 · 2026Article
- Towards a unified gating scheme for the CNBD ion channel family.The Journal of general physiology · 2026Review
- Tuning the gate and the gear: The LRRC26 (bioRxiv : the preprint server for biology · 2025Article
- CaNature communications · 2025Article
- Structural basis of voltage-dependent gating in BK channels.Nature communications · 2025Article
- Markov models and long-term memory in ion channels: A contradiction in terms?Biophysical journal · 2025Article
- The conductance of KCNQ2 and its pathogenic variants is determined by individual subunit gating.Science advances · 2025Article
- Distinct potassium channel types in brain capillary pericytes.Biophysical journal · 2024Article
- Evaluating sequential and allosteric activation models in IKs channels with mutated voltage sensors.The Journal of general physiology · 2024Article
- Purkinje cell models: past, present and future.Frontiers in computational neuroscience · 2024Review
- A gating lever and molecular logic gate that couple voltage and calcium sensor activation to opening in BK potassium channels.Science advances · 2022Article
- An allosteric modulator activates BK channels by perturbing coupling between CaNature communications · 2022Article
- The allosteric gating mechanism of the MthK channel.National science review · 2022Article
- To what extent naringenin binding and membrane depolarization shape mitoBK channel gating-A machine learning approach.PLoS computational biology · 2022Article
- Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021Review
- Article
- The Calcium Signaling Mechanisms in Arterial Smooth Muscle and Endothelial Cells.Comprehensive Physiology · 2021Article
- Goblet cell LRRC26 regulates BK channel activation and protects against colitis in mice.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Coronary Large Conductance CaFrontiers in physiology · 2021Review
113 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Large-conductance Ca-activated potassium channels (BK channels) are uniquely sensitive to both membrane potential and intracellular Ca2+. Recent work has demonstrated that in the gating of these channels there are voltage-sensitive steps that are separate from Ca2+ binding steps. Based on this result and the macroscopic steady state and kinetic properties of the cloned BK channel mslo, we have recently proposed a general kinetic scheme to describe the interaction between voltage and Ca2+ in the gating of the mslo channel (Cui, J., D.H. Cox, and R.W. Aldrich. 1997. J. Gen. Physiol. In press.). This scheme supposes that the channel exists in two main conformations, closed and open. The conformational change between closed and open is voltage dependent. Ca2+ binds to both the closed and open conformations, but on average binds more tightly to the open conformation and thereby promotes channel opening. Here we describe the basic properties of models of this form and test their ability to mimic mslo macroscopic steady state and kinetic behavior. The simplest form of this scheme corresponds to a voltage-dependent version of the Monod-Wyman-Changeux (MWC) model of allosteric proteins. The success of voltage-dependent MWC models in describing many aspects of mslo gating suggests that these channels may share a common molecular mechanism with other allosteric proteins whose behaviors have been modeled using the MWC formalism. We also demonstrate how this scheme can arise as a simplification of a more complex scheme that is based on the premise that the channel is a homotetramer with a single Ca2+ binding site and a single voltage sensor in each subunit. Aspects of the mslo data not well fitted by the simplified scheme will likely be better accounted for by this more general scheme. The kinetic schemes discussed in this paper may be useful in interpreting the effects of BK channel modifications or mutations.
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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.