ArticleBiophysical journal2010
Coupling between residues on S4 and S1 defines the voltage-sensor resting conformation in NaChBac.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 18 citations in OpenAlex.
- Allosteric interactions among voltage-sensor modules of sodium channels probed by scorpion toxin modifiers.Journal of neurobiology and physiology · 2022Article
- Charge substitutions at the voltage-sensing module of domain III enhance actions of site-3 and site-4 toxins on an insect sodium channel.Insect biochemistry and molecular biology · 2021Article
- Mapping the interaction surface of scorpion β-toxins with an insect sodium channel.The Biochemical journal · 2021Article
- Roles for Countercharge in the Voltage Sensor Domain of Ion Channels.Frontiers in pharmacology · 2020Review
- Cardiac Na Channels: Structure to Function.Current topics in membranes · 2016Article
- Modulation of a voltage-gated Na+ channel by sevoflurane involves multiple sites and distinct mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Asymmetric functional contributions of acidic and aromatic side chains in sodium channel voltage-sensor domains.The Journal of general physiology · 2014Article
- Hydrophobic plug functions as a gate in voltage-gated proton channels.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Insights on the mechanisms of Ca(2+) regulation of connexin26 hemichannels revealed by human pathogenic mutations (D50N/Y).The Journal of general physiology · 2013Article
- S1-S3 counter charges in the voltage sensor module of a mammalian sodium channel regulate fast inactivation.The Journal of general physiology · 2013Article
- Hinge-bending motions in the pore domain of a bacterial voltage-gated sodium channel.Biochimica et biophysica acta · 2012Article
- Gating charge interactions with the S1 segment during activation of a Na+ channel voltage sensor.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Arrangement and mobility of the voltage sensor domain in prokaryotic voltage-gated sodium channels.The Journal of biological chemistry · 2011Article
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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
The voltage sensor is a four-transmembrane helix bundle (S1-S4) that couples changes in membrane potential to conformational alterations in voltage-gated ion channels leading to pore opening and ion conductance. Although the structure of the voltage sensor in activated potassium channels is available, the conformation of the voltage sensor at rest is still obscure, limiting our understanding of the voltage-sensing mechanism. By employing a heterologously expressed Bacillus halodurans sodium channel (NaChBac), we defined constraints that affect the positioning and depolarization-induced outward motion of the S4 segment. We compared macroscopic currents mediated by NaChBac and mutants in which E43 on the S1 segment and the two outermost arginines (R1 and R2) on S4 were substituted. Neutralization of the negatively charged E43 (E43C) had a significant effect on channel gating. A double-mutant cycle analysis of E43 and R1 or R2 suggested changes in pairing during channel activation, implying that the interaction of E43 with R1 stabilizes the voltage sensor in its closed/available state, whereas interaction of E43 with R2 stabilizes the channel open/unavailable state. These constraints on S4 dynamics that define its stepwise movement upon channel activation and positioning at rest are novel, to the best of our knowledge, and compatible with the helical-screw and electrostatic models of S4 motion.
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