ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2010
Modulation of BK channel gating by the ß2 subunit involves both membrane-spanning and cytoplasmic domains of Slo1.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Circadian Control of Sleep by Melatonin via MTbioRxiv : the preprint server for biology · 2025Article
- Coupling of CaProceedings of the National Academy of Sciences of the United States of America · 2020Article
- 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
- 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
- Deletion of cytosolic gating ring decreases gate and voltage sensor coupling in BK channels.The Journal of general physiology · 2017Article
- Modulation of BK Channel Function by Auxiliary Beta and Gamma Subunits.International review of neurobiology · 2016Review
- Single Channel Recordings Reveal Differential β2 Subunit Modulations Between Mammalian and Drosophila BKCa(β2) Channels.PloS one · 2016Article
- N-terminal isoforms of the large-conductance Ca²⁺-activated K⁺ channel are differentially modulated by the auxiliary β1-subunit.The Journal of biological chemistry · 2014Article
- Functional insights into modulation of BKCa channel activity to alter myometrial contractility.Frontiers in physiology · 2014Review
- Both transmembrane domains of BK β1 subunits are essential to confer the normal phenotype of β1-containing BK channels.PloS one · 2014Article
- 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
- Integrative Approach for Computationally Inferring Interactions between the Alpha and Beta Subunits of the Calcium-Activated Potassium Channel (BK): a Docking Study.Bioinformatics and biology insights · 2013Article
- Inter-α/β subunits coupling mediating pre-inactivation and augmented activation of BKCa(β2).Scientific reports · 2013Article
- Modulation of BK channel voltage gating by different auxiliary β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Relative transmembrane segment rearrangements during BK channel activation resolved by structurally assigned fluorophore-quencher pairing.The Journal of general physiology · 2012Article
- Regulation of Voltage-Activated K(+) Channel Gating by Transmembrane β Subunits.Frontiers in pharmacology · 2012Article
- A BK (Slo1) channel journey from molecule to physiology.Channels (Austin, Tex.)Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Large-conductance, Ca(2+)- and voltage-sensitive K(+) (BK) channels regulate neuronal functions such as spike frequency adaptation and transmitter release. BK channels are composed of four Slo1 subunits, which contain the voltage-sensing and pore-gate domains in the membrane and Ca(2+) binding sites in the cytoplasmic domain, and accessory β subunits. Four types of BK channel β subunits (β1-β4) show differential tissue distribution and unique functional modulation, resulting in diverse phenotypes of BK channels. Previous studies show that both the β1 and β2 subunits increase Ca(2+) sensitivity, but different mechanisms may underline these modulations. However, the structural domains in Slo1 that are critical for Ca(2+)-dependent activation and targeted by these β subunits are not known. Here, we report that the N termini of both the transmembrane (including S0) and cytoplasmic domains of Slo1 are critical for β2 modulation based on the study of differential effects of the β2 subunit on two orthologs, mouse Slo1 and Drosophila Slo1. The N terminus of the cytoplasmic domain of Slo1, including the AC region (βA-αC) of the RCK1 (regulator of K(+) conductance) domain and the peptide linking it to S6, both of which have been shown previously to mediate the coupling between Ca(2+) binding and channel opening, is specifically required for the β2 but not for the β1 modulation. These results suggest that the β2 subunit modulates the coupling between Ca(2+) binding and channel opening, and, although sharing structural homology, the BK channel β subunits interact with structural domains in the Slo1 subunit differently to enhance channel activity.
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