ArticleProceedings of the National Academy of Sciences of the United States of America2010
Operation of the voltage sensor of a human voltage- and Ca2+-activated K+ channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026Review
- Structural basis of voltage-dependent gating in BK channels.Nature communications · 2025Article
- Fifty years of gating currents and channel gating.The Journal of general physiology · 2023Review
- Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021Review
- BK Channel Gating Mechanisms: Progresses Toward a Better Understanding of Variants Linked Neurological Diseases.Frontiers in physiology · 2021Review
- Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances.Nature communications · 2018Article
- Threading the biophysics of mammalian Slo1 channels onto structures of an invertebrate Slo1 channel.The Journal of general physiology · 2017Review
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- BK channels: multiple sensors, one activation gate.Frontiers in physiology · 2015Review
- Functional heterogeneity of the four voltage sensors of a human L-type calcium channel.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Modeling ion channels: past, present, and future.The Journal of general physiology · 2014Review
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Orientations and proximities of the extracellular ends of transmembrane helices S0 and S4 in open and closed BK potassium channels.PloS one · 2013Article
- A linkage analysis toolkit for studying allosteric networks in ion channels.The Journal of general physiology · 2013Article
- Relative transmembrane segment rearrangements during BK channel activation resolved by structurally assigned fluorophore-quencher pairing.The Journal of general physiology · 2012Article
- The contribution of RCK domains to human BK channel allosteric activation.The Journal of biological chemistry · 2012Article
- Worms take to the slo lane: a perspective on the mode of action of emodepside.Invertebrate neuroscience : IN · 2012Review
- Voltage sensor of ion channels and enzymes.Biophysical reviews · 2012Review
- Metal-driven operation of the human large-conductance voltage- and Ca2+-dependent potassium channel (BK) gating ring apparatus.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Voltage sensor domains (VSDs) are structurally and functionally conserved protein modules that consist of four transmembrane segments (S1-S4) and confer voltage sensitivity to many ion channels. Depolarization is sensed by VSD-charged residues residing in the membrane field, inducing VSD activation that facilitates channel gating. S4 is typically thought to be the principal functional component of the VSD because it carries, in most channels, a large portion of the VSD gating charge. The VSDs of large-conductance, voltage- and Ca(2+)-activated K(+) channels are peculiar in that more gating charge is carried by transmembrane segments other than S4. Considering its "decentralized" distribution of voltage-sensing residues, we probed the BK(Ca) VSD for evidence of cooperativity between charge-carrying segments S2 and S4. We achieved this by optically tracking their activation by using voltage clamp fluorometry, in channels with intact voltage sensors and charge-neutralized mutants. The results from these experiments indicate that S2 and S4 possess distinct voltage dependence, but functionally interact, such that the effective valence of one segment is affected by charge neutralization in the other. Statistical-mechanical modeling of the experimental findings using allosteric interactions demonstrates two mechanisms (mechanical coupling and dynamic focusing of the membrane electric field) that are compatible with the observed cross-segment effects of charge neutralization.
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