ArticleProceedings of the National Academy of Sciences of the United States of America2012
Modulation of BK channel voltage gating by different auxiliary β subunits.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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69 citing papers in PubMed, 109 citations in OpenAlex.
- Evolution towards higher unitary conductance in mammals makes BK channels more efficient and precise.Communications biology · 2026Article
- β2 and β3a regulatory subunits can coassemble in the same BK channels.The Journal of general physiology · 2026Article
- Smooth muscle of the lower urinary tract: BK-RyR coupling in physiology and pathophysiology.Journal of muscle research and cell motility · 2025Review
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- Tuning the gate and the gear: The LRRC26 (bioRxiv : the preprint server for biology · 2025Article
- Large conductance voltage-and calcium-activated KFrontiers in pharmacology · 2024Review
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- Lysosomal Potassium Channels.Handbook of experimental pharmacology · 2023Review
- Mapping the functional expression of auxiliary subunits of KScientific reports · 2022Article
- Mechanism of voltage sensing in CaProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cholinergic modulation of persistent inward currents is mediated by activating muscarinic receptors of serotonergic neurons in the brainstem of ePet-EYFP mice.Experimental brain research · 2022Article
- Effect of an autism-associatedCurrent research in physiology · 2022Article
- Differential Regulation of Gonadotropins as Revealed by Transcriptomes of Distinct LH and FSH Cells of Fish Pituitary.International journal of molecular sciences · 2021Article
- Application of Machine-Learning Methods to Recognize mitoBK Channels from Different Cell Types Based on the Experimental Patch-Clamp Results.International journal of molecular sciences · 2021Article
- The Membrane Cholesterol Modulates the Interaction Between 17-βEstradiol and the BK Channel.Frontiers in pharmacology · 2021Article
- Hypoxic Regulation of the Large-Conductance, Calcium and Voltage-Activated Potassium Channel, BK.Frontiers in physiology · 2021Review
- Neuropathic Pain in Multiple Sclerosis and Its Animal Models: Focus on Mechanisms, Knowledge Gaps and Future Directions.Frontiers in neurology · 2021Review
- The Large-Conductance, Calcium-Activated Potassium Channel: A Big Key Regulator of Cell Physiology.Frontiers in physiology · 2021Review
- High-Resolution Structures of KHandbook of experimental pharmacology · 2021Article
- Article
9 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calcium- and voltage-activated potassium channels (BK) are regulated by a multiplicity of signals. The prevailing view is that different BK gating mechanisms converge to determine channel opening and that these gating mechanisms are allosterically coupled. In most instances the pore forming α subunit of BK is associated with one of four alternative β subunits that appear to target specific gating mechanisms to regulate the channel activity. In particular, β1 stabilizes the active configuration of the BK voltage sensor having a large effect on BK Ca(2+) sensitivity. To determine the extent to which β subunits regulate the BK voltage sensor, we measured gating currents induced by the pore-forming BK α subunit alone and with the different β subunits expressed in Xenopus oocytes (β1, β2IR, β3b, and β4). We found that β1, β2, and β4 stabilize the BK voltage sensor in the active conformation. β3 has no effect on voltage sensor equilibrium. In addition, β4 decreases the apparent number of charges per voltage sensor. The decrease in the charge associated with the voltage sensor in α β4 channels explains most of their biophysical properties. For channels composed of the α subunit alone, gating charge increases slowly with pulse duration as expected if a significant fraction of this charge develops with a time course comparable to that of K(+) current activation. In the presence of β1, β2, and β4 this slow component develops in advance of and much more rapidly than ion current activation, suggesting that BK channel opening proceeds in two steps.
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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.