Roles for Countercharge in the Voltage Sensor Domain of Ion Channels
Abstract
Voltage-gated ion channels share a common structure typified by peripheral, voltage sensor domains. Their S4 segments respond to alteration in membrane potential with translocation coupled to ion permeation through a central pore domain. The mechanisms of gating in these channels have been intensely studied using pioneering methods such as measurement of charge displacement across a membrane, sequencing of genes coding for voltage-gated ion channels, and the development of all-atom molecular dynamics simulations using structural information from prokaryotic and eukaryotic channel proteins. One aspect of this work has been the description of the role of conserved negative countercharges in S1, S2, and S3 transmembrane segments to promote sequential salt-bridge formation with positively charged residues in S4 segments. These interactions facilitate S4 translocation through the lipid bilayer. In this review, we describe functional and computational work investigating the role of these countercharges in S4 translocation, voltage sensor domain hydration, and in diseases resulting from countercharge mutations.
- Authors:
-
- Idaho State Univ., Pocatello, ID (United States). Dept. of Biological Sciences
- Idaho State Univ., Pocatello, ID (United States). Dept. of Biological Sciences; Oregon Health and Sciences University School of Medicine, Portland, OR (United States)
- Publication Date:
- Research Org.:
- Idaho National Laboratory (INL), Idaho Falls, ID (United States)
- Sponsoring Org.:
- USDOE National Nuclear Security Administration (NNSA); National Institutes of Health (NIH); Idaho IDeA Network of Biomedical Research Excellence (INBRE); National Institute of General Medical Sciences (NIGMS); USDOE Office of Nuclear Energy (NE)
- OSTI Identifier:
- 1628212
- Grant/Contract Number:
- AC07-05ID14517; 1R15NS093579-01A1; P20GM103408
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Frontiers in Pharmacology
- Additional Journal Information:
- Journal Volume: 11; Journal ID: ISSN 1663-9812
- Publisher:
- Frontiers Research Foundation
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; pharmacology & pharmacy; countercharge; crystallography; electrostatic; ion channel; molecular dynamics; channelopathy; sliding helix model; voltage sensor domain
Citation Formats
Groome, James R., and Bayless-Edwards, Landon. Roles for Countercharge in the Voltage Sensor Domain of Ion Channels. United States: N. p., 2020.
Web. doi:10.3389/fphar.2020.00160.
Groome, James R., & Bayless-Edwards, Landon. Roles for Countercharge in the Voltage Sensor Domain of Ion Channels. United States. https://doi.org/10.3389/fphar.2020.00160
Groome, James R., and Bayless-Edwards, Landon. Fri .
"Roles for Countercharge in the Voltage Sensor Domain of Ion Channels". United States. https://doi.org/10.3389/fphar.2020.00160. https://www.osti.gov/servlets/purl/1628212.
@article{osti_1628212,
title = {Roles for Countercharge in the Voltage Sensor Domain of Ion Channels},
author = {Groome, James R. and Bayless-Edwards, Landon},
abstractNote = {Voltage-gated ion channels share a common structure typified by peripheral, voltage sensor domains. Their S4 segments respond to alteration in membrane potential with translocation coupled to ion permeation through a central pore domain. The mechanisms of gating in these channels have been intensely studied using pioneering methods such as measurement of charge displacement across a membrane, sequencing of genes coding for voltage-gated ion channels, and the development of all-atom molecular dynamics simulations using structural information from prokaryotic and eukaryotic channel proteins. One aspect of this work has been the description of the role of conserved negative countercharges in S1, S2, and S3 transmembrane segments to promote sequential salt-bridge formation with positively charged residues in S4 segments. These interactions facilitate S4 translocation through the lipid bilayer. In this review, we describe functional and computational work investigating the role of these countercharges in S4 translocation, voltage sensor domain hydration, and in diseases resulting from countercharge mutations.},
doi = {10.3389/fphar.2020.00160},
journal = {Frontiers in Pharmacology},
number = ,
volume = 11,
place = {United States},
year = {Fri Feb 28 00:00:00 EST 2020},
month = {Fri Feb 28 00:00:00 EST 2020}
}
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