Regulation of the cardiac Na+ channel NaV1.5 by post-translational modifications

The cardiac voltage-gated Na+ channel, NaV1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of the electrical impulse in the myocardium. Even subtle alterations of NaV1.5 function, as caused by mutations in its gene SCN5A, may lead to many d...

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Published in:Journal of molecular and cellular cardiology Vol. 82; pp. 36 - 47
Main Authors: Marionneau, Céline, Abriel, Hugues
Format: Journal Article
Language:English
Published: England Elsevier Ltd 01.05.2015
Elsevier
Series:Equipe 1
Subjects:
Acetylation
Animals
Arrhythmias
Cardiac NaV1.5 channels
Gene Expression Regulation
Glycosylation
Humans
Life Sciences
Mass Spectrometry
Methylation
Native proteomics
NAV1.5 Voltage-Gated Sodium Channel - genetics
NAV1.5 Voltage-Gated Sodium Channel - metabolism
Oxidation-Reduction
Phosphorylation
Post-translational modifications
Protein Processing, Post-Translational
Proteomics - methods
Ubiquitination
Ac
BrS
pS
PKB/Akt
pT
MS
LQTS
PKA
NaV α subunit
PTM
Redox
PKC
pY
Cardiac NaV1.5 channels
INaL
CaMKII
Post-translational modifications
Native proteomics
PI3K
SGK
Me
AMPK
INa
Arrhythmias
Cardiac Na(V)1.5 channels
Cardiac Na V 15 channels
ISSN:0022-2828, 1095-8584, 1095-8584
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Abstract The cardiac voltage-gated Na+ channel, NaV1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of the electrical impulse in the myocardium. Even subtle alterations of NaV1.5 function, as caused by mutations in its gene SCN5A, may lead to many different arrhythmic phenotypes in carrier patients. In addition, acquired malfunctions of NaV1.5 that are secondary to cardiac disorders such as heart failure and cardiomyopathies, may also play significant roles in arrhythmogenesis. While it is clear that the regulation of NaV1.5 protein expression and function tightly depends on genetic mechanisms, recent studies have demonstrated that NaV1.5 is the target of various post-translational modifications that are pivotal not only in physiological conditions, but also in disease. In this review, we examine the recent literature demonstrating glycosylation, phosphorylation by Protein Kinases A and C, Ca2+/Calmodulin-dependent protein Kinase II, Phosphatidylinositol 3-Kinase, Serum- and Glucocorticoid-inducible Kinases, Fyn and Adenosine Monophosphate-activated Protein Kinase, methylation, acetylation, redox modifications, and ubiquitylation of NaV1.5. Modern and sensitive mass spectrometry approaches, applied directly to channel proteins that were purified from native cardiac tissues, have enabled the determination of the precise location of post-translational modification sites, thus providing essential information for understanding the mechanistic details of these regulations. The current challenge is first, to understand the roles of these modifications on the expression and the function of NaV1.5, and second, to further identify other chemical modifications. It is postulated that the diversity of phenotypes observed with NaV1.5-dependent disorders may partially arise from the complex post-translational modifications of channel protein components. •The cardiac NaV1.5 channel is subject to PTMs whose roles are partially understood.•The majority of NaV1.5 PTM sites are located in the first loop of the channel.•The use of native channel proteomics is of high discovery and gain.•NaV1.5 PTMs contribute to cardiac disease, which may have therapeutic applications.
AbstractList The cardiac voltage-gated Na(+) channel, Na(V)1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of the electrical impulse in the myocardium. Even subtle alterations of Na(V)1.5 function, as caused by mutations in its gene SCN5A, may lead to many different arrhythmic phenotypes in carrier patients. In addition, acquired malfunctions of Na(V)1.5 that are secondary to cardiac disorders such as heart failure and cardiomyopathies, may also play significant roles in arrhythmogenesis. While it is clear that the regulation of Na(V)1.5 protein expression and function tightly depends on genetic mechanisms, recent studies have demonstrated that Na(V)1.5 is the target of various post-translational modifications that are pivotal not only in physiological conditions, but also in disease. In this review, we examine the recent literature demonstrating glycosylation, phosphorylation by Protein Kinases A and C, Ca(2+)/Calmodulin-dependent protein Kinase II, Phosphatidylinositol 3-Kinase, Serum- and Glucocorticoid-inducible Kinases, Fyn and Adenosine Monophosphate-activated Protein Kinase, methylation, acetylation, redox modifications, and ubiquitylation of Na(V)1.5. Modern and sensitive mass spectrometry approaches, applied directly to channel proteins that were purified from native cardiac tissues, have enabled the determination of the precise location of post-translational modification sites, thus providing essential information for understanding the mechanistic details of these regulations. The current challenge is first, to understand the roles of these modifications on the expression and the function of Na(V)1.5, and second, to further identify other chemical modifications. It is postulated that the diversity of phenotypes observed with Na(V)1.5-dependent disorders may partially arise from the complex post-translational modifications of channel protein components.
The cardiac voltage-gated Na+ channel, NaV1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of the electrical impulse in the myocardium. Even subtle alterations of NaV1.5 function, as caused by mutations in its gene SCN5A, may lead to many different arrhythmic phenotypes in carrier patients. In addition, acquired malfunctions of NaV1.5 that are secondary to cardiac disorders such as heart failure and cardiomyopathies, may also play significant roles in arrhythmogenesis. While it is clear that the regulation of NaV1.5 protein expression and function tightly depends on genetic mechanisms, recent studies have demonstrated that NaV1.5 is the target of various post-translational modifications that are pivotal not only in physiological conditions, but also in disease. In this review, we examine the recent literature demonstrating glycosylation, phosphorylation by Protein Kinases A and C, Ca2+/Calmodulin-dependent protein Kinase II, Phosphatidylinositol 3-Kinase, Serum- and Glucocorticoid-inducible Kinases, Fyn and Adenosine Monophosphate-activated Protein Kinase, methylation, acetylation, redox modifications, and ubiquitylation of NaV1.5. Modern and sensitive mass spectrometry approaches, applied directly to channel proteins that were purified from native cardiac tissues, have enabled the determination of the precise location of post-translational modification sites, thus providing essential information for understanding the mechanistic details of these regulations. The current challenge is first, to understand the roles of these modifications on the expression and the function of NaV1.5, and second, to further identify other chemical modifications. It is postulated that the diversity of phenotypes observed with NaV1.5-dependent disorders may partially arise from the complex post-translational modifications of channel protein components. •The cardiac NaV1.5 channel is subject to PTMs whose roles are partially understood.•The majority of NaV1.5 PTM sites are located in the first loop of the channel.•The use of native channel proteomics is of high discovery and gain.•NaV1.5 PTMs contribute to cardiac disease, which may have therapeutic applications.
The cardiac voltage-gated Na(+) channel, Na(V)1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of the electrical impulse in the myocardium. Even subtle alterations of Na(V)1.5 function, as caused by mutations in its gene SCN5A, may lead to many different arrhythmic phenotypes in carrier patients. In addition, acquired malfunctions of Na(V)1.5 that are secondary to cardiac disorders such as heart failure and cardiomyopathies, may also play significant roles in arrhythmogenesis. While it is clear that the regulation of Na(V)1.5 protein expression and function tightly depends on genetic mechanisms, recent studies have demonstrated that Na(V)1.5 is the target of various post-translational modifications that are pivotal not only in physiological conditions, but also in disease. In this review, we examine the recent literature demonstrating glycosylation, phosphorylation by Protein Kinases A and C, Ca(2+)/Calmodulin-dependent protein Kinase II, Phosphatidylinositol 3-Kinase, Serum- and Glucocorticoid-inducible Kinases, Fyn and Adenosine Monophosphate-activated Protein Kinase, methylation, acetylation, redox modifications, and ubiquitylation of Na(V)1.5. Modern and sensitive mass spectrometry approaches, applied directly to channel proteins that were purified from native cardiac tissues, have enabled the determination of the precise location of post-translational modification sites, thus providing essential information for understanding the mechanistic details of these regulations. The current challenge is first, to understand the roles of these modifications on the expression and the function of Na(V)1.5, and second, to further identify other chemical modifications. It is postulated that the diversity of phenotypes observed with Na(V)1.5-dependent disorders may partially arise from the complex post-translational modifications of channel protein components.The cardiac voltage-gated Na(+) channel, Na(V)1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of the electrical impulse in the myocardium. Even subtle alterations of Na(V)1.5 function, as caused by mutations in its gene SCN5A, may lead to many different arrhythmic phenotypes in carrier patients. In addition, acquired malfunctions of Na(V)1.5 that are secondary to cardiac disorders such as heart failure and cardiomyopathies, may also play significant roles in arrhythmogenesis. While it is clear that the regulation of Na(V)1.5 protein expression and function tightly depends on genetic mechanisms, recent studies have demonstrated that Na(V)1.5 is the target of various post-translational modifications that are pivotal not only in physiological conditions, but also in disease. In this review, we examine the recent literature demonstrating glycosylation, phosphorylation by Protein Kinases A and C, Ca(2+)/Calmodulin-dependent protein Kinase II, Phosphatidylinositol 3-Kinase, Serum- and Glucocorticoid-inducible Kinases, Fyn and Adenosine Monophosphate-activated Protein Kinase, methylation, acetylation, redox modifications, and ubiquitylation of Na(V)1.5. Modern and sensitive mass spectrometry approaches, applied directly to channel proteins that were purified from native cardiac tissues, have enabled the determination of the precise location of post-translational modification sites, thus providing essential information for understanding the mechanistic details of these regulations. The current challenge is first, to understand the roles of these modifications on the expression and the function of Na(V)1.5, and second, to further identify other chemical modifications. It is postulated that the diversity of phenotypes observed with Na(V)1.5-dependent disorders may partially arise from the complex post-translational modifications of channel protein components.
Author Marionneau, Céline
Abriel, Hugues
Author_xml – sequence: 1
  givenname: Céline
  surname: Marionneau
  fullname: Marionneau, Céline
  email: celine.marionneau@univ-nantes.fr
  organization: L'institut du thorax, Institut National de la Santé et de la Recherche Médicale, Unité Mixte de Recherche 1087, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 6291, Université de Nantes, Nantes, France
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  givenname: Hugues
  surname: Abriel
  fullname: Abriel, Hugues
  email: Hugues.Abriel@dkf.unibe.ch
  organization: Department of Clinical Research, University of Bern, Bern, Switzerland
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ID FETCH-LOGICAL-c426t-d4e7c0a564bba6f2cb9a865dd163c38a43e2856871ab2bfc9db43d5445e3a5b13
ISSN 0022-2828
1095-8584
IngestDate Sat Nov 29 15:04:12 EST 2025
Thu Oct 02 05:10:09 EDT 2025
Thu Apr 03 07:09:08 EDT 2025
Sat Nov 29 06:14:22 EST 2025
Tue Nov 18 22:23:41 EST 2025
Fri Feb 23 02:20:34 EST 2024
Tue Oct 14 19:29:03 EDT 2025
IsPeerReviewed true
IsScholarly true
Keywords Ac
BrS
pS
PKB/Akt
pT
MS
LQTS
PKA
NaV α subunit
PTM
Redox
PKC
pY
Cardiac NaV1.5 channels
INaL
CaMKII
Post-translational modifications
Native proteomics
PI3K
SGK
Me
AMPK
INa
Arrhythmias
Cardiac Na(V)1.5 channels
Cardiac Na V 15 channels
Language English
License Copyright © 2015 Elsevier Ltd. All rights reserved.
Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0
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MergedId FETCHMERGED-LOGICAL-c426t-d4e7c0a564bba6f2cb9a865dd163c38a43e2856871ab2bfc9db43d5445e3a5b13
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
ORCID 0000-0003-0962-9756
PMID 25748040
PQID 1687995401
PQPubID 23479
PageCount 12
ParticipantIDs hal_primary_oai_HAL_hal_01830583v1
proquest_miscellaneous_1687995401
pubmed_primary_25748040
crossref_citationtrail_10_1016_j_yjmcc_2015_02_013
crossref_primary_10_1016_j_yjmcc_2015_02_013
elsevier_sciencedirect_doi_10_1016_j_yjmcc_2015_02_013
elsevier_clinicalkey_doi_10_1016_j_yjmcc_2015_02_013
PublicationCentury 2000
PublicationDate May 2015
2015-05-00
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PublicationDateYYYYMMDD 2015-05-01
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  year: 2015
  text: May 2015
PublicationDecade 2010
PublicationPlace England
PublicationPlace_xml – name: England
PublicationSeriesTitle Equipe 1
PublicationTitle Journal of molecular and cellular cardiology
PublicationTitleAlternate J Mol Cell Cardiol
PublicationYear 2015
Publisher Elsevier Ltd
Elsevier
Publisher_xml – name: Elsevier Ltd
– name: Elsevier
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Snippet The cardiac voltage-gated Na+ channel, NaV1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of the...
The cardiac voltage-gated Na(+) channel, Na(V)1.5, is responsible for the upstroke of the action potential in cardiomyocytes and for efficient propagation of...
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SubjectTerms Acetylation
Animals
Arrhythmias
Cardiac NaV1.5 channels
Gene Expression Regulation
Glycosylation
Humans
Life Sciences
Mass Spectrometry
Methylation
Native proteomics
NAV1.5 Voltage-Gated Sodium Channel - genetics
NAV1.5 Voltage-Gated Sodium Channel - metabolism
Oxidation-Reduction
Phosphorylation
Post-translational modifications
Protein Processing, Post-Translational
Proteomics - methods
Ubiquitination
Title Regulation of the cardiac Na+ channel NaV1.5 by post-translational modifications
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https://dx.doi.org/10.1016/j.yjmcc.2015.02.013
https://www.ncbi.nlm.nih.gov/pubmed/25748040
https://www.proquest.com/docview/1687995401
https://hal.science/hal-01830583
Volume 82
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