ArticleThe Journal of general physiology2005
Differential effects of beta 1 and beta 2 subunits on BK channel activity.
Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed, 136 citations in OpenAlex.
- Pharmacological Relevance of β-, γ-, and LINGO Auxiliary Subunits in BK Channel Modulation.ChemMedChem · 2026Review
- Article
- 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
- The BK channel-NS1619 agonist complex reveals molecular insights into allosteric activation gating.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- β2 and β3a regulatory subunits can coassemble in the same BK channels.The Journal of general physiology · 2026Article
- Tuning the gate and the gear: The LRRC26 (bioRxiv : the preprint server for biology · 2025Article
- The Slo1 Y450F Substitution Modifies Basal Function and Cholesterol Response of Middle Cerebral Artery Smooth Muscle BK Channels in a Sexually Dimorphic Manner.International journal of molecular sciences · 2025Article
- Activation mechanism and novel binding sites of the BKLife science alliance · 2024Article
- Challenges in the Therapeutic Targeting of KCa Channels: From Basic Physiology to Clinical Applications.International journal of molecular sciences · 2024Review
- Large conductance voltage-and calcium-activated KFrontiers in pharmacology · 2024Review
- Novel Thioxothiazolo[3,4-ACS medicinal chemistry letters · 2022Article
- Regulatory mechanisms of mitochondrial BKChannels (Austin, Tex.) · 2021Review
- Hypoxic Regulation of the Large-Conductance, Calcium and Voltage-Activated Potassium Channel, BK.Frontiers in physiology · 2021Review
- The Membrane Cholesterol Modulates the Interaction Between 17-βEstradiol and the BK Channel.Frontiers in pharmacology · 2021Article
- Calcium-Activated KHandbook of experimental pharmacology · 2021Article
- FeACS chemical biology · 2020Article
- Pro-inflammatory Cytokines Drive Deregulation of Potassium Channel Expression in Primary Synovial Fibroblasts.Frontiers in physiology · 2020Article
- Rectification ratio based determination of disulfide bonds of β2 extracellular loop of BK channel.Channels (Austin, Tex.) · 2019Article
- The molecular nature of the 17β-Estradiol binding site in the voltage- and CaScientific reports · 2019Article
- Emerging roles for multifunctional ion channel auxiliary subunits in cancer.Cell calcium · 2019Review
38 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High conductance, calcium- and voltage-activated potassium (BK) channels are widely expressed in mammals. In some tissues, the biophysical properties of BK channels are highly affected by coexpression of regulatory (beta) subunits. beta1 and beta2 subunits increase apparent channel calcium sensitivity. The beta1 subunit also decreases the voltage sensitivity of the channel and the beta2 subunit produces an N-type inactivation of BK currents. We further characterized the effects of the beta1 and beta2 subunits on the calcium and voltage sensitivity of the channel, analyzing the data in the context of an allosteric model for BK channel activation by calcium and voltage (Horrigan and Aldrich, 2002). In this study, we used a beta2 subunit without its N-type inactivation domain (beta2IR). The results indicate that the beta2IR subunit, like the beta1 subunit, has a small effect on the calcium binding affinity of the channel. Unlike the beta1 subunit, the beta2IR subunit also has no effect on the voltage sensitivity of the channel. The limiting voltage dependence for steady-state channel activation, unrelated to voltage sensor movements, is unaffected by any of the studied beta subunits. The same is observed for the limiting voltage dependence of the deactivation time constant. Thus, the beta1 subunit must affect the voltage sensitivity by altering the function of the voltage sensors of the channel. Both beta subunits reduce the intrinsic equilibrium constant for channel opening (L0). In the allosteric activation model, the reduction of the voltage dependence for the activation of the voltage sensors accounts for most of the macroscopic steady-state effects of the beta1 subunit, including the increase of the apparent calcium sensitivity of the BK channel. All allosteric coupling factors need to be increased in order to explain the observed effects when the alpha subunit is coexpressed with the beta2IR subunit.
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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.