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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Veröffentlicht in:	Journal of molecular and cellular cardiology Jg. 82; S. 36 - 47
Hauptverfasser:	Marionneau, Céline, Abriel, Hugues
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	England Elsevier Ltd 01.05.2015 Elsevier
Schriftenreihe:	Equipe 1
Schlagworte:	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 – sequence: 2 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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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
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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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