ArticleThe Journal of general physiology2002
Slo1 tail domains, but not the Ca2+ bowl, are required for the beta 1 subunit to increase the apparent Ca2+ sensitivity of BK channels.
Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- SLO3: A Conserved Regulator of Sperm Membrane Potential.International journal of molecular sciences · 2023Review
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- 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
- Article
- Of fish oil, rafts, and scrambling things up.The Journal of general physiology · 2013Article
- The interface between membrane-spanning and cytosolic domains in Ca²+-dependent K+ channels is involved in β subunit modulation of gating.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Distinct sensitivity of slo1 channel proteins to ethanol.Molecular pharmacology · 2013Article
- The BK channel: a vital link between cellular calcium and electrical signaling.Protein & cell · 2012Review
- Role of KCNMA1 in breast cancer.PloS one · 2012Article
- Ginsenoside Rg3 enhances large conductance Ca2+-activated potassium channel currents: a role of Tyr360 residue.Molecules and cells · 2011Article
- On benzofuroindole analogues as smooth muscle relaxants.Journal of biomedicine & biotechnology · 2011Review
- Highly specific alternative splicing of transcripts encoding BK channels in the chicken's cochlea is a minor determinant of the tonotopic gradient.Molecular and cellular biology · 2010Article
- Inactivation of the KcsA potassium channel explored with heterotetramers.The Journal of general physiology · 2010Article
- Mechanism of increased BK channel activation from a channel mutation that causes epilepsy.The Journal of general physiology · 2009Article
- Measuring the influence of the BKCa {beta}1 subunit on Ca2+ binding to the BKCa channel.The Journal of general physiology · 2009Article
- Article
- Locations of the beta1 transmembrane helices in the BK potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Subunit-specific effect of the voltage sensor domain on Ca2+ sensitivity of BK channels.Biophysical journal · 2008Article
- Regulation of STREX exon large conductance, calcium-activated potassium channels by the beta4 accessory subunit.Neuroscience · 2007Article
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Authors and funding
5 authors.
Funding
Abstract
Functional large-conductance Ca(2+)- and voltage-activated K(+) (BK) channels can be assembled from four alpha subunits (Slo1) alone, or together with four auxiliary beta1 subunits to greatly increase the apparent Ca(2+) sensitivity of the channel. We examined the structural features involved in this modulation with two types of experiments. In the first, the tail domain of the alpha subunit, which includes the RCK2 (regulator of K(+) conductance) domain and Ca(2+) bowl, was replaced with the tail domain of Slo3, a BK-related channel that lacks both a Ca(2+) bowl and high affinity Ca(2+) sensitivity. In the second, the Ca(2+) bowl was disrupted by mutations that greatly reduce the apparent Ca(2+) sensitivity. We found that the beta1 subunit increased the apparent Ca(2+) sensitivity of Slo1 channels, independently of whether the alpha subunits were expressed as separate cores (S0-S8) and tails (S9-S10) or full length, and this increase was still observed after the Ca(2+) bowl was mutated. In contrast, beta1 subunits no longer increased Ca(2+) sensitivity when Slo1 tails were replaced by Slo3 tails. The beta1 subunits were still functionally coupled to channels with Slo3 tails, as DHS-I and 17 beta-estradiol activated these channels in the presence of beta1 subunits, but not in their absence. These findings indicate that the increase in apparent Ca(2+) sensitivity induced by the beta1 subunit does not require either the Ca(2+) bowl or the linker between the RCK1 and RCK2 domains, and that Slo3 tails cannot substitute for Slo1 tails. The beta1 subunit also induced a decrease in voltage sensitivity that occurred with either Slo1 or Slo3 tails. In contrast, the beta1 subunit-induced increase in apparent Ca(2+) sensitivity required Slo1 tails. This suggests that the allosteric activation pathways for these two types of actions of the beta1 subunit may be different.
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