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We identify a human mutation (E1053K) in the ankyrin-binding motif of Na(v)1.5 that is associated with Brugada syndrome, a fatal cardiac arrhythmia caused by altered function of Na(v)1.5. The E1053K mutation abolishes binding of Na(v)1.5 to ankyrin-G, and also prevents accumulation of Na(v)1.5 at cell surface sites in ventricular cardiomyocytes. Ankyrin-G and Na(v)1.5 are both localized at intercalated disc and T-tubule membranes in cardiomyocytes, and Na(v)1.5 coimmunoprecipitates with 190-kDa ankyrin-G from detergent-soluble lysates from rat heart. These data suggest that Na(v)1.5 associates with ankyrin-G and that ankyrin-G is required for Na(v)1.5 localization at excitable membranes in cardiomyocytes. Together with previous work in neurons, these results in cardiomyocytes suggest that ankyrin-G participates in a common pathway for localization of voltage-gated Na(v) channels at sites of function in multiple excitable cell types.

proceedings of the national academy of sciences of the united states of america

Na <sub>v</sub> 1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Na <sub>v</sub> 1.5 on the surface of cardiomyocytes

Na v 1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Na v 1.5 on the surface of cardiomyocytes

Na _v 1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Na _v 1.5 on the surface of cardiomyocytes