ReviewThe Journal of physiology2010
Allosteric interactions and the modular nature of the voltage- and Ca2+-activated (BK) channel.
Review in The Journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- From venom peptides to neurotherapeutics: BmK defensins and short-chain peptides as modulators of ion channels.Frontiers in pharmacology · 2026Review
- Closed state structure of the pore revealed by uncoupled Shaker KNature communications · 2025Article
- Toluene is a cerebral artery constrictor acting via BK channels.Neuropharmacology · 2025Article
- The role and mechanism of vascular wall cell ion channels in vascular fibrosis remodeling.Channels (Austin, Tex.) · 2024Review
- Large conductance voltage-and calcium-activated KFrontiers in pharmacology · 2024Review
- Routes for Potassium Ions across Mitochondrial Membranes: A Biophysical Point of View with Special Focus on the ATP-Sensitive KBiomolecules · 2021Review
- BK in Double-Membrane Organelles: A Biophysical, Pharmacological, and Functional Survey.Frontiers in physiology · 2021Review
- Comparative gain-of-function effects of theJournal of neurophysiology · 2020Article
- MitoBKThe Journal of physiology · 2019Article
- Peptide toxins and small-molecule blockers of BK channels.Acta pharmacologica Sinica · 2016Review
- Oxidative Stress and Maxi Calcium-Activated Potassium (BK) Channels.Biomolecules · 2015Review
- BK channels: multiple sensors, one activation gate.Frontiers in physiology · 2015Review
- Impairment of brain mitochondrial charybdotoxin- and ATP-insensitive BK channel activities in diabetes.Neuromolecular medicine · 2014Article
- Large conductance calcium-activated potassium channels: their expression and modulation of glutamate release from nerve terminals isolated from rat trigeminal caudal nucleus and cerebral cortex.Neurochemical research · 2014Article
- BK channel opening involves side-chain reorientation of multiple deep-pore residues.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The smooth muscle-type β1 subunit potentiates activation by DiBAC4(3) in recombinant BK channels.Channels (Austin, Tex.) · 2014Article
- Both transmembrane domains of BK β1 subunits are essential to confer the normal phenotype of β1-containing BK channels.PloS one · 2014Article
- Pharmacological consequences of the coexpression of BK channel α and auxiliary β subunits.Frontiers in physiology · 2014Review
- Single-channel kinetics of BK (Slo1) channels.Frontiers in physiology · 2014Review
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The high conductance voltage- and Ca(2+)-activated K(+) channel is one of the most broadly expressed channels in mammals. This channel is named BK for 'big K' because of its single-channel conductance that can be as large as 250 pS in 100 mm symmetrical K(+). BK channels increase their activity by membrane depolarization or an increase in cytosolic Ca(2+). One of the key features that defines the behaviour of BK channels is that neither Ca(2+) nor voltage is strictly necessary for channel activation. This and several other observations led to the idea that both Ca(2+) and voltage increase the open probability by an allosteric mechanism. In this type of mechanism, the processes of voltage sensor displacement, Ca(2+) binding and pore opening are independent equilibria that interact allosterically with each other. These allosteric interactions in BK channels reside in the structural characteristics of the BK channel in the sense that voltage and Ca(2+) sensors and the pore need to be contained in different structures or 'modules'. Through electrophysiological, mutagenesis, biochemical and fluorescence studies these modules have been identified and, more important, some of the interactions between them have been unveiled. In this review, we have covered the main advances achieved during the last few years in the elucidation of the structure of the BK channel and how this is related with its function as an allosteric protein.
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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.