ArticleThe Journal of general physiology2012
An extracellular domain of the accessory β1 subunit is required for modulating BK channel voltage sensor and gate.
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 22 papers.
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Who cites it
22 citing papers in PubMed.
- In vivo mapping of protein-protein interactions of schizophrenia risk factors generates an interconnected disease network.Schizophrenia (Heidelberg, Germany) · 2026Article
- Modulation of potassium channels by transmembrane auxiliary subunits via voltage-sensing domains.Physiological reports · 2024Review
- Effect of an autism-associatedCurrent research in physiology · 2022Article
- Molecular structures of the human Slo1 KeLife · 2019Article
- BK β1 subunit-dependent facilitation of ethanol inhibition of BK current and cerebral artery constriction is mediated by the β1 transmembrane domain 2.British journal of pharmacology · 2017Article
- Association between potassium channel SNPs and essential hypertension in Xinjiang Kazak Chinese patients.Experimental and therapeutic medicine · 2017Article
- The unique N-terminal sequence of the BKCa channel α-subunit determines its modulation by β-subunits.PloS one · 2017Article
- Alcohol modulation of BK channel gating depends on β subunit composition.The Journal of general physiology · 2016Article
- Modulation of BK Channel Function by Auxiliary Beta and Gamma Subunits.International review of neurobiology · 2016Review
- Molecular mechanism underlying β1 regulation in voltage- and calcium-activated potassium (BK) channels.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Tungstate-targeting of BKαβ1 channels tunes ERK phosphorylation and cell proliferation in human vascular smooth muscle.PloS one · 2015Article
- BK channel activation by tungstate requires the β1 subunit extracellular loop residues essential to modulate voltage sensor function and channel gating.Pflugers Archiv : European journal of physiology · 2014Article
- Conopeptide Vt3.1 preferentially inhibits BK potassium channels containing β4 subunits via electrostatic interactions.The Journal of biological chemistry · 2014Article
- Both transmembrane domains of BK β1 subunits are essential to confer the normal phenotype of β1-containing BK channels.PloS one · 2014Article
- Article
- The interface between membrane-spanning and cytosolic domains in Ca²+-dependent K+ channels is involved in β subunit modulation of gating.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Positions of β2 and β3 subunits in the large-conductance calcium- and voltage-activated BK potassium channel.The Journal of general physiology · 2013Article
- Orientations and proximities of the extracellular ends of transmembrane helices S0 and S4 in open and closed BK potassium channels.PloS one · 2013Article
- Regulation of Voltage-Activated K(+) Channel Gating by Transmembrane β Subunits.Frontiers in pharmacology · 2012Article
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3 authors.
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Abstract
A family of tissue-specific auxiliary β subunits modulates large conductance voltage- and calcium-activated potassium (BK) channel gating properties to suit their diverse functions. Paradoxically, β subunits both promote BK channel activation through a stabilization of voltage sensor activation and reduce BK channel openings through an increased energetic barrier of the closed-to-open transition. The molecular determinants underlying β subunit function, including the dual gating effects, remain unknown. In this study, we report the first identification of a β1 functional domain consisting of Y74, S104, Y105, and I106 residues located in the extracellular loop of β1. These amino acids reside within two regions of highest conservation among related β1, β2, and β4 subunits. Analysis in the context of the Horrigan-Aldrich gating model revealed that this domain functions to both promote voltage sensor activation and also reduce intrinsic gating. Free energy calculations suggest that the dual effects of the β1 Y74 and S104-I106 domains can be largely accounted for by a relative destabilization of channels in open states that have few voltage sensors activated. These results suggest a unique and novel mechanism for β subunit modulation of voltage-gated potassium channels wherein interactions between extracellular β subunit residues with the external portions of the gate and voltage sensor regulate channel opening.
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