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

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Beltrán Álvarez, Pedro
orcId Feixas Geronès, Ferran​ researcherId Feixas Geronès, Ferran​ scopusId Feixas Geronès, Ferran​ ​
Feixas Geronès, Ferran
orcId Osuna Oliveras, Sílvia​ researcherId Osuna Oliveras, Sílvia​ scopusId Osuna Oliveras, Sílvia​ ​
Osuna Oliveras, Sílvia
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Díaz Hernández, Rubí
orcId Brugada, Ramon​ ​ scopusId Brugada, Ramon​ ​
Brugada, Ramon
orcId Pagans i Lista, Sara​ researcherId Pagans i Lista, Sara​ scopusId Pagans i Lista, Sara​ ​
Pagans i Lista, Sara
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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 ​
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