ArticleThe Journal of general physiology2012
Relative transmembrane segment rearrangements during BK channel activation resolved by structurally assigned fluorophore-quencher pairing.
Article in The Journal of general physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026Review
- Article
- A rich conformational palette underlies human CaNature communications · 2025Article
- Article
- Article
- Displacement of the NaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- BK Channel Gating Mechanisms: Progresses Toward a Better Understanding of Variants Linked Neurological Diseases.Frontiers in physiology · 2021Review
- The Large-Conductance, Calcium-Activated Potassium Channel: A Big Key Regulator of Cell Physiology.Frontiers in physiology · 2021Review
- Article
- Harnessing photoinduced electron transfer to optically determine protein sub-nanoscale atomic distances.Nature communications · 2018Article
- Mechanisms of noncovalent β subunit regulation of NaThe Journal of general physiology · 2017Article
- Using fluorescence to understand β subunit-NaThe Journal of general physiology · 2017Article
- Conformational dynamics and role of the acidic pocket in ASIC pH-dependent gating.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Interactions of divalent cations with calcium binding sites of BK channels reveal independent motions within the gating ring.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- 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
- Extracellular Subunit Interactions Control Transitions between Functional States of Acid-sensing Ion Channel 1a.The Journal of biological chemistry · 2015Article
- How to open a proton pore-more than S4?Nature structural & molecular biology · 2015Article
- 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
- International Union of Basic and Clinical Pharmacology. XC. multisite pharmacology: recommendations for the nomenclature of receptor allosterism and allosteric ligands.Pharmacological reviews · 2014Article
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2 authors.
Funding
Abstract
Voltage-activated proteins can sense, and respond to, changes in the electric field pervading the cell membrane by virtue of a transmembrane helix bundle, the voltage-sensing domain (VSD). Canonical VSDs consist of four transmembrane helices (S1-S4) of which S4 is considered a principal component because it possesses charged residues immersed in the electric field. Membrane depolarization compels the charges, and by extension S4, to rearrange with respect to the field. The VSD of large-conductance voltage- and Ca-activated K(+) (BK) channels exhibits two salient inconsistencies from the canonical VSD model: (1) the BK channel VSD possesses an additional nonconserved transmembrane helix (S0); and (2) it exhibits a "decentralized" distribution of voltage-sensing charges, in helices S2 and S3, in addition to S4. Considering these unique features, the voltage-dependent rearrangements of the BK VSD could differ significantly from the standard model of VSD operation. To understand the mode of operation of this unique VSD, we have optically tracked the relative motions of the BK VSD transmembrane helices during activation, by manipulating the quenching environment of site-directed fluorescent labels with native and introduced Trp residues. Having previously reported that S0 and S4 diverge during activation, in this work we demonstrate that S4 also diverges from S1 and S2, whereas S2, compelled by its voltage-sensing charged residues, moves closer to S1. This information contributes spatial constraints for understanding the BK channel voltage-sensing process, revealing the structural rearrangements in a non-canonical VSD.
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