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A new look at sodium channel β subunits
Voltage-gated sodium (Na(v)) channels are intrinsic plasma membrane proteins that initiate the action potential in electrically excitable cells. They are a major focus of research in neurobiology, structural biology, membrane biology and pharmacology. Mutations in Na(v) channels are implicated in a...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4313373/ https://www.ncbi.nlm.nih.gov/pubmed/25567098 http://dx.doi.org/10.1098/rsob.140192 |
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author | Namadurai, Sivakumar Yereddi, Nikitha R. Cusdin, Fiona S. Huang, Christopher L.-H. Chirgadze, Dimitri Y. Jackson, Antony P. |
author_facet | Namadurai, Sivakumar Yereddi, Nikitha R. Cusdin, Fiona S. Huang, Christopher L.-H. Chirgadze, Dimitri Y. Jackson, Antony P. |
author_sort | Namadurai, Sivakumar |
collection | PubMed |
description | Voltage-gated sodium (Na(v)) channels are intrinsic plasma membrane proteins that initiate the action potential in electrically excitable cells. They are a major focus of research in neurobiology, structural biology, membrane biology and pharmacology. Mutations in Na(v) channels are implicated in a wide variety of inherited pathologies, including cardiac conduction diseases, myotonic conditions, epilepsy and chronic pain syndromes. Drugs active against Na(v) channels are used as local anaesthetics, anti-arrhythmics, analgesics and anti-convulsants. The Na(v) channels are composed of a pore-forming α subunit and associated β subunits. The β subunits are members of the immunoglobulin (Ig) domain family of cell-adhesion molecules. They modulate multiple aspects of Na(v) channel behaviour and play critical roles in controlling neuronal excitability. The recently published atomic resolution structures of the human β3 and β4 subunit Ig domains open a new chapter in the study of these molecules. In particular, the discovery that β3 subunits form trimers suggests that Na(v) channel oligomerization may contribute to the functional properties of some β subunits. |
format | Online Article Text |
id | pubmed-4313373 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-43133732015-02-10 A new look at sodium channel β subunits Namadurai, Sivakumar Yereddi, Nikitha R. Cusdin, Fiona S. Huang, Christopher L.-H. Chirgadze, Dimitri Y. Jackson, Antony P. Open Biol Review Voltage-gated sodium (Na(v)) channels are intrinsic plasma membrane proteins that initiate the action potential in electrically excitable cells. They are a major focus of research in neurobiology, structural biology, membrane biology and pharmacology. Mutations in Na(v) channels are implicated in a wide variety of inherited pathologies, including cardiac conduction diseases, myotonic conditions, epilepsy and chronic pain syndromes. Drugs active against Na(v) channels are used as local anaesthetics, anti-arrhythmics, analgesics and anti-convulsants. The Na(v) channels are composed of a pore-forming α subunit and associated β subunits. The β subunits are members of the immunoglobulin (Ig) domain family of cell-adhesion molecules. They modulate multiple aspects of Na(v) channel behaviour and play critical roles in controlling neuronal excitability. The recently published atomic resolution structures of the human β3 and β4 subunit Ig domains open a new chapter in the study of these molecules. In particular, the discovery that β3 subunits form trimers suggests that Na(v) channel oligomerization may contribute to the functional properties of some β subunits. The Royal Society 2015-01-07 /pmc/articles/PMC4313373/ /pubmed/25567098 http://dx.doi.org/10.1098/rsob.140192 Text en http://creativecommons.org/licenses/by/4.0/ © 2015 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Review Namadurai, Sivakumar Yereddi, Nikitha R. Cusdin, Fiona S. Huang, Christopher L.-H. Chirgadze, Dimitri Y. Jackson, Antony P. A new look at sodium channel β subunits |
title | A new look at sodium channel β subunits |
title_full | A new look at sodium channel β subunits |
title_fullStr | A new look at sodium channel β subunits |
title_full_unstemmed | A new look at sodium channel β subunits |
title_short | A new look at sodium channel β subunits |
title_sort | new look at sodium channel β subunits |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4313373/ https://www.ncbi.nlm.nih.gov/pubmed/25567098 http://dx.doi.org/10.1098/rsob.140192 |
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