ArticleThe Journal of general physiology2008
Measurements of the BKCa channel's high-affinity Ca2+ binding constants: effects of membrane voltage.
Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed.
- Potential therapeutic targeting of BKMolecular oncology · 2026Review
- Structural basis of voltage-dependent gating in BK channels.Nature communications · 2025Article
- Challenges in the Therapeutic Targeting of KCa Channels: From Basic Physiology to Clinical Applications.International journal of molecular sciences · 2024Review
- Hypoxia, Ion Channels and Glioblastoma Malignancy.Biomolecules · 2023Review
- CaInternational journal of molecular sciences · 2023Review
- A gating lever and molecular logic gate that couple voltage and calcium sensor activation to opening in BK potassium channels.Science advances · 2022Article
- Structure of the Human BK Ion Channel in Lipid Environment.Membranes · 2022Article
- State-dependent inhibition of BK channels by the opioid agonist loperamide.The Journal of general physiology · 2021Article
- BK Channel Gating Mechanisms: Progresses Toward a Better Understanding of Variants Linked Neurological Diseases.Frontiers in physiology · 2021Review
- Calcium-Activated KHandbook of experimental pharmacology · 2021Article
- FeACS chemical biology · 2020Article
- Coupling of CaProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Comparative gain-of-function effects of theJournal of neurophysiology · 2020Article
- Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site.eLife · 2019Article
- Article
- Efficiency measures the conversion of agonist binding energy into receptor conformational change.The Journal of general physiology · 2019Article
- Article
- Molecular determinants of CaScientific reports · 2018Article
- Threading the biophysics of mammalian Slo1 channels onto structures of an invertebrate Slo1 channel.The Journal of general physiology · 2017Review
- Large-conductance CaThe Journal of physiology · 2017Article
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2 authors.
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Abstract
It has been established that the large conductance Ca(2+)-activated K(+) channel contains two types of high-affinity Ca(2+) binding sites, termed the Ca(2+) bowl and the RCK1 site. The affinities of these sites, and how they change as the channel opens, is still a subject of some debate. Previous estimates of these affinities have relied on fitting a series of conductance-voltage relations determined over a series of Ca(2+) concentrations with models of channel gating that include both voltage sensing and Ca(2+) binding. This approach requires that some model of voltage sensing be chosen, and differences in the choice of voltage-sensing model may underlie the different estimates that have been produced. Here, to better determine these affinities we have measured Ca(2+) dose-response curves of channel activity at constant voltage for the wild-type mSlo channel (minus its low-affinity Ca(2+) binding site) and for channels that have had one or the other Ca(2+) binding site disabled via mutation. To accurately determine these dose-response curves we have used a series of 22 Ca(2+) concentrations, and we have used unitary current recordings, coupled with changes in channel expression level, to measure open probability over five orders of magnitude. Our results indicate that at -80 mV the Ca(2+) bowl has higher affinity for Ca(2+) than does the RCK1 site in both the opened and closed conformations of the channel, and that the binding of Ca(2+) to the RCK1 site is voltage dependent, whereas at the Ca(2+) bowl it is not.
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Registered trials
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.