Journal
AMINO ACIDS
Volume 47, Issue 2, Pages 429-434Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-014-1890-0
Keywords
Sodium channel; Post-translational modification; Arginine methylation; Phosphorylation; Cross-talk
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Funding
- Fundacio Obra Social La Caixa, Spanish Government [SAF2011-27627, CTQ2011-25086/BQU)]
- European Community [PCIG14-GA-2013-630978]
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Arginine methylation is a novel post-translational modification within the voltage-gated ion channel superfamily, including the cardiac sodium channel, Na(V)1.5. We show that Na(V)1.5 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. Na(V)1.5 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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