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C-terminal phosphorylation of NaV1.5 impairs FGF13-dependent regulation of channel inactivation

Burel, Sophie, Coyan, Fabien C., Lorenzini, Maxime, Meyer, Matthew R., Lichti, Cheryl F., Brown, Joan H., Loussouarn, Gildas , Charpentier, Flavien , Nerbonne, Jeanne M., Townsend, R. Reid, Maier, Lars S. and Marionneau, Céline (2017) C-terminal phosphorylation of NaV1.5 impairs FGF13-dependent regulation of channel inactivation. Journal of Biological Chemistry 292 (42), pp. 17431-17448.

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Other URL: http://doi.org/10.1074/jbc.M117.787788


Abstract

Voltage-gated Na+ (Na-V) channels are key regulators of myocardial excitability, and Ca2+/calmodulin-dependent protein kinase II (CaMKII)-dependent alterations in Na(V)1.5 channel inactivation are emerging as a critical determinant of arrhythmias in heart failure. However, the global native phosphorylation pattern of Na(V)1.5 subunits associated with these arrhythmogenic disorders and the ...

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Item type:Article
Date:2017
Institutions:Medicine > Lehrstuhl für Innere Medizin II
Identification Number:
ValueType
10.1074/jbc.M117.787788DOI
Keywords:FACTOR HOMOLOGOUS FACTOR; LATE SODIUM CURRENT; HEART-FAILURE; KINASE-II; MASS-SPECTROMETRY; NA+ CHANNELS; QUANTITATIVE-ANALYSIS; MEMBRANE-PROTEINS; STATISTICAL-MODEL; CRYSTAL-STRUCTURE;
Dewey Decimal Classification:600 Technology > 610 Medical sciences Medicine
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:39663
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