ArticleProceedings of the National Academy of Sciences of the United States of America2015
Molecular mechanism underlying β1 regulation in voltage- and calcium-activated potassium (BK) channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Potential therapeutic targeting of BKMolecular oncology · 2026Review
- β2 and β3a regulatory subunits can coassemble in the same BK channels.The Journal of general physiology · 2026Article
- Tmem45b modulates itch via endoplasmic reticulum calcium regulation.Frontiers in physiology · 2025Article
- A Transcriptomic Comparative Study of Cranial Vasculature.Translational stroke research · 2024Article
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- Glycosylation of β1 subunit plays a pivotal role in the toxin sensitivity and activation of BK channels.The journal of venomous animals and toxins including tropical diseases · 2021Article
- Calcium-Activated KHandbook of experimental pharmacology · 2021Article
- Control of Biophysical and Pharmacological Properties of Potassium Channels by Ancillary Subunits.Handbook of experimental pharmacology · 2021Article
- Hypoxic Regulation of the Large-Conductance, Calcium and Voltage-Activated Potassium Channel, BK.Frontiers in physiology · 2021Review
- The Sodium Channel B4-Subunits are Dysregulated in Temporal Lobe Epilepsy Drug-Resistant Patients.International journal of molecular sciences · 2020Article
- Molecular structures of the human Slo1 KeLife · 2019Article
- The molecular nature of the 17β-Estradiol binding site in the voltage- and CaScientific reports · 2019Article
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- 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
- Distinct domains of the β1-subunit cytosolic N terminus control surface expression and functional properties of large-conductance calcium-activated potassium (BK) channels.The Journal of biological chemistry · 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
- 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
- Modulation of BK Channel Function by Auxiliary Beta and Gamma Subunits.International review of neurobiology · 2016Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Being activated by depolarizing voltages and increases in cytoplasmic Ca(2+), voltage- and calcium-activated potassium (BK) channels and their modulatory β-subunits are able to dampen or stop excitatory stimuli in a wide range of cellular types, including both neuronal and nonneuronal tissues. Minimal alterations in BK channel function may contribute to the pathophysiology of several diseases, including hypertension, asthma, cancer, epilepsy, and diabetes. Several gating processes, allosterically coupled to each other, control BK channel activity and are potential targets for regulation by auxiliary β-subunits that are expressed together with the α (BK)-subunit in almost every tissue type where they are found. By measuring gating currents in BK channels coexpressed with chimeras between β1 and β3 or β2 auxiliary subunits, we were able to identify that the cytoplasmic regions of β1 are responsible for the modulation of the voltage sensors. In addition, we narrowed down the structural determinants to the N terminus of β1, which contains two lysine residues (i.e., K3 and K4), which upon substitution virtually abolished the effects of β1 on charge movement. The mechanism by which K3 and K4 stabilize the voltage sensor is not electrostatic but specific, and the α (BK)-residues involved remain to be identified. This is the first report, to our knowledge, where the regulatory effects of the β1-subunit have been clearly assigned to a particular segment, with two pivotal amino acids being responsible for this modulation.
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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.