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Interplay between R513 methylation and S516 phosphorylation of the cardiac voltage-gated sodium channel

Arginine methylation is a novel post-translational modification within the voltage-gated ion channel superfamily, including the cardiac sodium channel, Nav1.5. We show that Nav1.5 R513 methylation decreases S516 phosphorylation rate by 4 orders of magnitude, the first evidence of protein kinase A inhibition by arginine methylation. Reciprocally, S516 phosphorylation blocks R513 methylation. Nav1.5 p.G514C, associated to cardiac conduction disease, abrogates R513 methylation, while leaving S516 phosphorylation rate unchanged. This is the first report of methylation-phosphorylation cross-talk of a cardiac ion channel

Springer Verlag

Director: Ministerio de Ciencia e Innovación (Espanya)
Autor: Beltrán-Álvarez, Pedro
Feixas Geronès, Ferran
Osuna Oliveras, Sílvia
Díaz-Hernández, Rubí
Brugada, Ramon
Pagans i Lista, Sara
Resum: Arginine methylation is a novel post-translational modification within the voltage-gated ion channel superfamily, including the cardiac sodium channel, Nav1.5. We show that Nav1.5 R513 methylation decreases S516 phosphorylation rate by 4 orders of magnitude, the first evidence of protein kinase A inhibition by arginine methylation. Reciprocally, S516 phosphorylation blocks R513 methylation. Nav1.5 p.G514C, associated to cardiac conduction disease, abrogates R513 methylation, while leaving S516 phosphorylation rate unchanged. This is the first report of methylation-phosphorylation cross-talk of a cardiac ion channel
Accés al document: http://hdl.handle.net/2072/295648
Llenguatge: eng
Editor: Springer Verlag
Drets: Tots els drets reservats
Matèria: Sodium channel
Arginina -- Metilació
Arginine -- Methylation
Fosforilació
Phosphorylation
Títol: Interplay between R513 methylation and S516 phosphorylation of the cardiac voltage-gated sodium channel
Tipus: info:eu-repo/semantics/article
Repositori: Recercat

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