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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

Manager: Ministerio de Ciencia e Innovación (Espanya)
Author: Beltrán-Álvarez, Pedro
Feixas Geronès, Ferran
Osuna Oliveras, Sílvia
Díaz-Hernández, Rubí
Brugada, Ramon
Pagans i Lista, Sara
Abstract: 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
Document access: http://hdl.handle.net/2072/295648
Language: eng
Publisher: Springer Verlag
Rights: Tots els drets reservats
Subject: Sodium channel
Arginina -- Metilació
Arginine -- Methylation
Fosforilació
Phosphorylation
Title: Interplay between R513 methylation and S516 phosphorylation of the cardiac voltage-gated sodium channel
Type: info:eu-repo/semantics/article
Repository: Recercat

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