Key result
Proteomic analysis identified arginine methylation at R513, R526, and R680 as a novel post-translational modification of the cardiac sodium channel Na(v)1.5.
Answers are grounded in this paper and cite their sources.
This study identifies arginine methylation as a novel post-translational modification of the cardiac sodium channel Na(v)1.5, with potential implications for understanding the mechanisms of Brugada and long QT type 3 syndromes.
The α subunit of the cardiac sodium channel (Na(v)1.5) is an essential protein in the initial depolarization phase of the cardiomyocyte action potential. Post-translational modifications such as phosphorylation are known to regulate Na(v)1.5 function. Here, we used a proteomic approach for the study of the post-translational modifications of Na(v)1.5 using tsA201 cells as a model system. We generated a stable cell line expressing Na(v)1.5, purified the sodium channel, and analyzed Na(v)1.5 by MALDI-TOF and LC-MS/MS. We report the identification of arginine methylation as a novel post-translational modification of Na(v)1.5. R513, R526, and R680, located in the linker between domains I and II in Na(v)1.5, were found in mono- or dimethylated states. The functional relevance of arginine methylation in Na(v)1.5 is underscored by the fact that R526H and R680H are known Na(v)1.5 mutations causing Brugada and long QT type 3 syndromes, respectively. Our work describes for the first time arginine methylation in the voltage-gated ion channel superfamily.
No takes yet. Share an insight, caveat, or question.
Beltrán-Álvarez et al. (2011) studied this question. Proteomic analysis identified arginine methylation at R513, R526, and R680 as a novel post-translational modification of the cardiac sodium channel Na(v)1.5.
Synapse has enriched 10 related papers. Consider them for comparative context: