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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...

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Autores principales: Namadurai, Sivakumar, Yereddi, Nikitha R., Cusdin, Fiona S., Huang, Christopher L.-H., Chirgadze, Dimitri Y., Jackson, Antony P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2015
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.
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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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