Posttranslational regulation of cardiac NaV1.5 channels is critical in modulating channel expression and function, yet their regulation by phosphorylation of accessory proteins has gone largely unexplored. Using phosphoproteomic analysis of NaV channel complexes from adult mouse left ventricles, we identified nine phosphorylation sites on intracellular fibroblast growth factor 13 (iFGF13).
View Article and Find Full Text PDFBackground: Brugada syndrome is a significant cause of sudden cardiac death (SCD), but the underlying mechanisms remain hypothetical.
Objectives: This study aimed to elucidate this knowledge gap through detailed ex vivo human heart studies.
Methods: A heart was obtained from a 15-year-old adolescent boy with normal electrocardiogram who experienced SCD.
Unlabelled: Phosphorylation of the cardiac Na 1.5 channel pore-forming subunit is extensive and critical in modulating channel expression and function, yet the regulation of Na 1.5 by phosphorylation of its accessory proteins remains elusive.
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