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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
Open accessAbstract
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.
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Citations
Cites
Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden cardiac death
Mohler, P. J., Schott, J.-J., Gramolini, A. O., Dilly, K. W., Guatimosim, S., duBell, W. H., Song, L.-S., Haurogné, K., Kyndt, F., Ali, M. E., et al. (2003) · Nature · doi:10.1038/nature01335 · Cited by 957
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Cited by
Fishman, G. I., Chugh, S. S., DiMarco, J. P., Albert, C. M., Anderson, M. E., Bonow, R. O., Buxton, A. E., Chen, P.-S., Estes, M., Jouven, X., et al. (2010) · Circulation · doi:10.1161/circulationaha.110.976092 · Cited by 614
ter Keurs, H. E. D. J., & Boyden, P. A. (2007) · Physiological Reviews · doi:10.1152/physrev.00011.2006 · Cited by 356
Cardiac Sodium Channel ( SCN5A ) Variants Associated with Atrial Fibrillation
Darbar, D., Kannankeril, P. J., Donahue, B. S., Kucera, G., Stubblefield, T., Haines, J. L., George, A. L., & Roden, D. M. (2008) · Circulation · doi:10.1161/circulationaha.107.757955 · Cited by 334
Cardiac sodium channel Nav1.5 and interacting proteins: Physiology and pathophysiology
Abriel, H. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.08.025 · Cited by 268
CUNHA, S., & MOHLER, P. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.03.018 · Cited by 65
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Metadata
- Authors
- Mohler, P. J., Rivolta, I., Napolitano, C., LeMaillet, G., Lambert, S., Priori, S. G., & Bennett, V.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-12-03
- Volume
- 101
- Issue
- 50
- Pages
- 17533-17538
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2134798732
- Cited by
- 360
- References
- 1
- FWCI
- 11.15
- Type
- journal article
- Language
- en
- Open access
- green
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- Mohler, P. J., Rivolta, I., Napolitano, C., LeMaillet, G., Lambert, S., Priori, S. G., & Bennett, V. (2004). 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. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0403711101
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