ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2009
Location of the beta 4 transmembrane helices in the BK potassium channel.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2009. 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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31 citing papers in PubMed.
- Development of charybdotoxin Q18F variant as a selective peptide blocker of neuronal BK(α + β4) channel for the treatment of epileptic seizures.Protein science : a publication of the Protein Society · 2022Article
- Molecular structures of the human Slo1 KeLife · 2019Article
- Rectification ratio based determination of disulfide bonds of β2 extracellular loop of BK channel.Channels (Austin, Tex.) · 2019Article
- Solution structure of extracellular loop of human β4 subunit of BK channel and its biological implication on ChTX sensitivity.Scientific reports · 2018Article
- BK β1 subunit-dependent facilitation of ethanol inhibition of BK current and cerebral artery constriction is mediated by the β1 transmembrane domain 2.British journal of pharmacology · 2017Article
- Alcohol modulation of BK channel gating depends on β subunit composition.The Journal of general physiology · 2016Article
- Modulation of BK Channel Function by Auxiliary Beta and Gamma Subunits.International review of neurobiology · 2016Review
- Two classes of regulatory subunits coassemble in the same BK channel and independently regulate gating.Nature communications · 2015Article
- 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
- Two distinct effects of PIP2 underlie auxiliary subunit-dependent modulation of Slo1 BK channels.The Journal of general physiology · 2015Article
- Positions of the cytoplasmic end of BK α S0 helix relative to S1-S6 and of β1 TM1 and TM2 relative to S0-S6.The Journal of general physiology · 2015Article
- S-acylation dependent post-translational cross-talk regulates large conductance calcium- and voltage- activated potassium (BK) channels.Frontiers in physiology · 2014Review
- Pharmacological consequences of the coexpression of BK channel α and auxiliary β subunits.Frontiers in physiology · 2014Review
- Both transmembrane domains of BK β1 subunits are essential to confer the normal phenotype of β1-containing BK channels.PloS one · 2014Article
- Palmitoylation of the β4-subunit regulates surface expression of large conductance calcium-activated potassium channel splice variants.The Journal of biological chemistry · 2013Article
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Mechanism of the modulation of BK potassium channel complexes with different auxiliary subunit compositions by the omega-3 fatty acid DHA.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Orientations and proximities of the extracellular ends of transmembrane helices S0 and S4 in open and closed BK potassium channels.PloS one · 2013Article
- Inter-α/β subunits coupling mediating pre-inactivation and augmented activation of BKCa(β2).Scientific reports · 2013Article
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12 authors.
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Abstract
Large-conductance, voltage- and Ca(2+)-gated potassium (BK) channels control excitability in a number of cell types. BK channels are composed of alpha subunits, which contain the voltage-sensor domains and the Ca(2+)- sensor domains and form the pore, and often one of four types of beta subunits, which modulate the channel in a cell-specific manner. beta 4 is expressed in neurons throughout the brain. Deletion of beta 4 in mice causes temporal lobe epilepsy. Compared with channels composed of alpha alone, channels composed of alpha and beta 4 activate and deactivate more slowly. We inferred the locations of the two beta 4 transmembrane (TM) helices TM1 and TM2 relative to the seven alpha TM helices, S0-S6, from the extent of disulfide bond formation between cysteines substituted in the extracellular flanks of these TM helices. We found that beta 4 TM2 is close to alpha S0 and that beta 4 TM1 is close to both alpha S1 and S2. At least at their extracellular ends, TM1 and TM2 are not close to S3-S6. In six of eight of the most highly crosslinked cysteine pairs, four crosslinks from TM2 to S0 and one each from TM1 to S1 and S2 had small effects on the V(50) and on the rates of activation and deactivation. That disulfide crosslinking caused only small functional perturbations is consistent with the proximity of the extracellular ends of TM2 to S0 and of TM1 to S1 and to S2, in both the open and closed states.
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