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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

Authors

Ferran Feixas

Sílvia Osuna

Rubí Díaz-Hernández

Ramon Brugada

Sara Pagans



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.

Journal Article Type Article
Publication Date 2015-02
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
APA6 Citation 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. https://doi.org/10.1007/s00726-014-1890-0
DOI https://doi.org/10.1007/s00726-014-1890-0
Keywords Sodium channel; Post-translational modification; Arginine methylation; Phosphorylation; Cross-talk
Publisher URL http://link.springer.com/article/10.1007%2Fs00726-014-1890-0
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 http://dx.doi.org/10.1007/s00726-014-1890-0

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