ArticleThe Journal of general physiology2012
Selectivity filter gating in large-conductance Ca(2+)-activated K+ channels.
Article in The Journal of general physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Article
- 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
- Mechanism of use-dependent Kv2 channel inhibition by RY785.The Journal of general physiology · 2022Article
- Selectivity filter ion binding affinity determines inactivation in a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Molecular mechanism of BK channel activation by the smooth muscle relaxant NS11021.The Journal of general physiology · 2020Article
- Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- LRET Determination of Molecular Distances during pH Gating of the Mammalian Inward Rectifier Kir1.1b.Biophysical journal · 2018Article
- Threading the biophysics of mammalian Slo1 channels onto structures of an invertebrate Slo1 channel.The Journal of general physiology · 2017Review
- Molecular mechanisms of Slo2 KThe Journal of physiology · 2017Article
- Article
- Closed state-coupled C-type inactivation in BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Individual Ion Binding Sites in the K(+) Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation.Structure (London, England : 1993) · 2016Article
- Voltage-Gated Potassium Channels: A Structural Examination of Selectivity and Gating.Cold Spring Harbor perspectives in biology · 2016Review
- Calcium ions open a selectivity filter gate during activation of the MthK potassium channel.Nature communications · 2015Article
- Cadmium-cysteine coordination in the BK inner pore region and its structural and functional implications.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Hydrophobic gating in ion channels.Journal of molecular biology · 2015Review
- Probing binding sites and mechanisms of action of an I(Ks) activator by computations and experiments.Biophysical journal · 2015Article
- Hydrophobic interaction between contiguous residues in the S6 transmembrane segment acts as a stimuli integration node in the BK channel.The Journal of general physiology · 2015Article
- Oxidative modulation of voltage-gated potassium channels.Antioxidants & redox signaling · 2014Review
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2 authors.
Funding
Abstract
Membrane voltage controls the passage of ions through voltage-gated K (K(v)) channels, and many studies have demonstrated that this is accomplished by a physical gate located at the cytoplasmic end of the pore. Critical to this determination were the findings that quaternary ammonium ions and certain peptides have access to their internal pore-blocking sites only when the channel gates are open, and that large blocking ions interfere with channel closing. Although an intracellular location for the physical gate of K(v) channels is well established, it is not clear if such a cytoplasmic gate exists in all K(+) channels. Some studies on large-conductance, voltage- and Ca(2+)-activated K(+) (BK) channels suggest a cytoplasmic location for the gate, but other findings question this conclusion and, instead, support the concept that BK channels are gated by the pore selectivity filter. If the BK channel is gated by the selectivity filter, the interactions between the blocking ions and channel gating should be influenced by the permeant ion. Thus, we tested tetrabutyl ammonium (TBA) and the Shaker "ball" peptide (BP) on BK channels with either K(+) or Rb(+) as the permeant ion. When tested in K(+) solutions, both TBA and the BP acted as open-channel blockers of BK channels, and the BP interfered with channel closing. In contrast, when Rb(+) replaced K(+) as the permeant ion, TBA and the BP blocked both closed and open BK channels, and the BP no longer interfered with channel closing. We also tested the cytoplasmically gated Shaker K channels and found the opposite behavior: the interactions of TBA and the BP with these K(v) channels were independent of the permeant ion. Our results add significantly to the evidence against a cytoplasmic gate in BK channels and represent a positive test for selectivity filter gating.
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