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

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


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Dr Pedro Beltran-Alvarez
Senior Lecturer in Health and Climate Change and Programme co-Director of the MSc Health and Climate Change

Ferran Feixas

Sílvia Osuna

Rubí Díaz-Hernández

Ramon Brugada

Sara Pagans


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.


Beltran-Alvarez, P., Feixas, F., Osuna, S., Díaz-Hernández, R., Brugada, R., & Pagans, S. (2015). Interplay between R513 methylation and S516 phosphorylation of the cardiac voltage-gated sodium channel. Amino acids, 47(2), 429-434.

Journal Article Type Article
Acceptance Date Dec 4, 2014
Online Publication Date Dec 16, 2014
Publication Date 2015-02
Deposit Date Mar 11, 2016
Publicly Available Date Mar 11, 2016
Journal Amino acids
Print ISSN 0939-4451
Electronic ISSN 1438-2199
Publisher Springer Verlag
Peer Reviewed Peer Reviewed
Volume 47
Issue 2
Pages 429-434
Keywords Sodium channel; Post-translational modification; Arginine methylation; Phosphorylation; Cross-talk
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Additional Information Author's accepted manuscript of article published in: Amino acids, 2014, v.47, issue 2. The final publication is available at Springer via


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