Referenced in: none

Automatically associated channels: Nav1.5

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

Authors: Pedro Beltran-Alvarez, Ferran Feixas, Sílvia Osuna, Rubí Díaz-Hernández, Ramon Brugada, Sara Pagans

Journal, date & volume: Amino Acids, 2015 Feb , 47, 429-34

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/25501501

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.