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Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals
The voltage sensor domain (VSD) has long been studied as a unique domain intrinsic to voltage-gated ion channels (VGICs). Within VGICs, the VSD is tightly coupled to the pore-gate domain (PGD) in diverse ways suitable for its specific function in each physiological context, including action potentia...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Japan Academy
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6541726/ https://www.ncbi.nlm.nih.gov/pubmed/30853698 http://dx.doi.org/10.2183/pjab.95.010 |
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author | OKAMURA, Yasushi OKOCHI, Yoshifumi |
author_facet | OKAMURA, Yasushi OKOCHI, Yoshifumi |
author_sort | OKAMURA, Yasushi |
collection | PubMed |
description | The voltage sensor domain (VSD) has long been studied as a unique domain intrinsic to voltage-gated ion channels (VGICs). Within VGICs, the VSD is tightly coupled to the pore-gate domain (PGD) in diverse ways suitable for its specific function in each physiological context, including action potential generation, muscle contraction and relaxation, hormone and neurotransmitter secretion, and cardiac pacemaking. However, some VSD-containing proteins lack a PGD. Voltage-sensing phosphatase contains a cytoplasmic phosphoinositide phosphatase with similarity to phosphatase and tensin homolog (PTEN). H(v)1, a voltage-gated proton channel, also lacks a PGD. Within H(v)1, the VSD operates as a voltage sensor, gate, and pore for both proton sensing and permeation. H(v)1 has a C-terminal coiled coil that mediates dimerization for cooperative gating. Recent progress in the structural biology of VGICs and VSD proteins provides insights into the principles of VSD coupling conserved among these proteins as well as the hierarchy of protein organization for voltage-evoked cell signaling. |
format | Online Article Text |
id | pubmed-6541726 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The Japan Academy |
record_format | MEDLINE/PubMed |
spelling | pubmed-65417262019-06-11 Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals OKAMURA, Yasushi OKOCHI, Yoshifumi Proc Jpn Acad Ser B Phys Biol Sci Review The voltage sensor domain (VSD) has long been studied as a unique domain intrinsic to voltage-gated ion channels (VGICs). Within VGICs, the VSD is tightly coupled to the pore-gate domain (PGD) in diverse ways suitable for its specific function in each physiological context, including action potential generation, muscle contraction and relaxation, hormone and neurotransmitter secretion, and cardiac pacemaking. However, some VSD-containing proteins lack a PGD. Voltage-sensing phosphatase contains a cytoplasmic phosphoinositide phosphatase with similarity to phosphatase and tensin homolog (PTEN). H(v)1, a voltage-gated proton channel, also lacks a PGD. Within H(v)1, the VSD operates as a voltage sensor, gate, and pore for both proton sensing and permeation. H(v)1 has a C-terminal coiled coil that mediates dimerization for cooperative gating. Recent progress in the structural biology of VGICs and VSD proteins provides insights into the principles of VSD coupling conserved among these proteins as well as the hierarchy of protein organization for voltage-evoked cell signaling. The Japan Academy 2019-03-11 /pmc/articles/PMC6541726/ /pubmed/30853698 http://dx.doi.org/10.2183/pjab.95.010 Text en © 2019 The Japan Academy This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review OKAMURA, Yasushi OKOCHI, Yoshifumi Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals |
title | Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals |
title_full | Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals |
title_fullStr | Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals |
title_full_unstemmed | Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals |
title_short | Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals |
title_sort | molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6541726/ https://www.ncbi.nlm.nih.gov/pubmed/30853698 http://dx.doi.org/10.2183/pjab.95.010 |
work_keys_str_mv | AT okamurayasushi molecularmechanismsofcouplingtovoltagesensorsinvoltageevokedcellularsignals AT okochiyoshifumi molecularmechanismsofcouplingtovoltagesensorsinvoltageevokedcellularsignals |