ArticleThe Journal of general physiology2009
Measuring the influence of the BKCa {beta}1 subunit on Ca2+ binding to the BKCa channel.
Article in The Journal of general physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Tuning the gate and the gear: The LRRC26 (γ1) subunit modulates intrinsic gating and voltage-sensor coupling of the BK channel.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Tuning the gate and the gear: The LRRC26 (bioRxiv : the preprint server for biology · 2025Article
- Piezo1, the new actor in cell volume regulation.Pflugers Archiv : European journal of physiology · 2024Review
- How Merkel cells transduce mechanical stimuli: A biophysical model of Merkel cells.PLoS computational biology · 2023Article
- Fifty years of gating currents and channel gating.The Journal of general physiology · 2023Review
- Potassium Ion Channels in Glioma: From Basic Knowledge into Therapeutic Applications.Membranes · 2023Review
- Review
- Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021Review
- The Large-Conductance, Calcium-Activated Potassium Channel: A Big Key Regulator of Cell Physiology.Frontiers in physiology · 2021Review
- MitoBKThe Journal of physiology · 2019Article
- The molecular nature of the 17β-Estradiol binding site in the voltage- and CaScientific reports · 2019Article
- Article
- Activation of human smooth muscle BK channels by hydrochlorothiazide requires cell integrity and the presence of BK βActa pharmacologica Sinica · 2018Article
- Physiological Roles and Therapeutic Potential of CaFrontiers in molecular neuroscience · 2018Review
- Statin therapy exacerbates alcohol-induced constriction of cerebral arteries via modulation of ethanol-induced BK channel inhibition in vascular smooth muscle.Biochemical pharmacology · 2017Article
- Association between potassium channel SNPs and essential hypertension in Xinjiang Kazak Chinese patients.Experimental and therapeutic medicine · 2017Article
- Membrane depolarization activates BK channels through ROCK-mediated β1 subunit surface trafficking to limit vasoconstriction.Science signaling · 2017Article
- Alcohol modulation of BK channel gating depends on β subunit composition.The Journal of general physiology · 2016Article
- 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
- Arachidonic acid activation of BKCa (Slo1) channels associated to the β1-subunit in human vascular smooth muscle cells.Pflugers Archiv : European journal of physiology · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The large-conductance Ca(2+)-activated potassium (BK(Ca)) channel of smooth muscle is unusually sensitive to Ca(2+) as compared with the BK(Ca) channels of brain and skeletal muscle. This is due to the tissue-specific expression of the BK(Ca) auxiliary subunit beta1, whose presence dramatically increases both the potency and efficacy of Ca(2+) in promoting channel opening. beta1 contains no Ca(2+) binding sites of its own, and thus the mechanism by which it increases the BK(Ca) channel's Ca(2+) sensitivity has been of some interest. Previously, we demonstrated that beta1 stabilizes voltage sensor activation, such that activation occurs at more negative voltages with beta1 present. This decreases the work that Ca(2+) must do to open the channel and thereby increases the channel's apparent Ca(2+) affinity without altering the real affinities of the channel's Ca(2+) binding sites. To explain the full effect of beta1 on the channel's Ca(2+) sensitivity, however, we also proposed that there must be effects of beta1 on Ca(2+) binding. Here, to test this hypothesis, we have used high-resolution Ca(2+) dose-response curves together with binding site-specific mutations to measure the effects of beta1 on Ca(2+) binding. We find that coexpression of beta1 alters Ca(2+) binding at both of the BK(Ca) channel's two types of high-affinity Ca(2+) binding sites, primarily increasing the affinity of the RCK1 sites when the channel is open and decreasing the affinity of the Ca(2+) bowl sites when the channel is closed. Both of these modifications increase the difference in affinity between open and closed, such that Ca(2+) binding at either site has a larger effect on channel opening when beta1 is present.
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