ArticleBiophysical journal2008
A residue at the cytoplasmic entrance of BK-type channels regulating single-channel opening by its hydrophobicity.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Effects of emodepside on single-channel properties of Onchocerca volvulus SLO-1A (BK) potassium channels.Parasites & vectors · 2025Article
- Single Channel Recordings Reveal Differential β2 Subunit Modulations Between Mammalian and Drosophila BKCa(β2) Channels.PloS one · 2016Article
- Amelogenin in Enamel Tissue Engineering.Advances in experimental medicine and biology · 2015Article
- Amelogenin as a Promoter of Nucleation and Crystal Growth of Apatite.Journal of crystal growth · 2011Article
- Intersubunit coupling in the pore of BK channels.The Journal of biological chemistry · 2009Article
- Lysine-rich extracellular rings formed by hbeta2 subunits confer the outward rectification of BK channels.PloS one · 2008Article
- A mutually exclusive alternative exon of slo1 codes for a neuronal BK channel with altered function.Channels (Austin, Tex.)Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single large-conductance calcium-activated K(+) (BK) channels encoded by the mSlo gene usually have synchronous gating, but a Drosophila dSlo (A2/C2/E2/G5/10) splice variant (dSlo1A) exhibits very flickery openings. To probe this difference in gating, we constructed a mutant I323T. This channel exhibits four subconductance levels similar to those of dSlo1A. Rectification of the single-channel current-voltage relation of I323T decreased as [Ca(2+) ](in) increased from 10 to 300 microM. Mutagenesis suggests that the hydrophobicity of the residue at the position is important for the wild-type gating; i.e., increasing hydrophobicity prolongs open duration. Molecular dynamics simulation suggests that four hydrophobic pore-lining residues at position 323 of mSlo act cooperatively in a "shutter-like" mechanism gating the permeation of K(+) ions. Rate-equilibrium free energy relations analysis shows that the four I323 residues in an mSlo channel have a conformation 65% similar to the closed conformation during gating. Based on these observations, we suggest that the appearance of rectification and substates of BK-type channels arise from a reduction of the cooperativity among these four residues and a lower probability of being open.
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