Voltage-Gated Sodium Channel Phosphorylation at Ser571 Regulates Late Current, Arrhythmia, and Cardiac Function In Vivo | Zendy

Patric Glynn | Zendy; Hassan Musa | Zendy; Xiangqiong Wu | Zendy; Sathya D. Unudurthi | Zendy; Sean C. Little | Zendy; Lan Qian | Zendy; Patrick Wright | Zendy; Przemysław Radwański | Zendy; Sándor Györke | Zendy; Peter J. Mohler | Zendy; Thomas J. Hund | Zendy

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Voltage-Gated Sodium Channel Phosphorylation at Ser571 Regulates Late Current, Arrhythmia, and Cardiac Function In Vivo

Author(s) -

Patric Glynn,

Hassan Musa,

Xiangqiong Wu,

Sathya D. Unudurthi,

Sean C. Little,

Lan Qian,

Patrick Wright,

Przemysław Radwański,

Sándor Györke,

Peter J. Mohler,

Thomas J. Hund

Publication year - 2015

Publication title -

circulation

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.795

H-Index - 607

eISSN - 1524-4539

pISSN - 0009-7322

DOI - 10.1161/circulationaha.114.015218

Subject(s) - phosphorylation , sodium channel , in vivo , repolarization , activator (genetics) , electrophysiology , microbiology and biotechnology , calmodulin , intracellular , biophysics , membrane potential , medicine , myocyte , protein kinase a , biology , chemistry , sodium , receptor , calcium , genetics , organic chemistry

Voltage-gated Na(+) channels (Nav) are essential for myocyte membrane excitability and cardiac function. Nav current (INa) is a large-amplitude, short-duration spike generated by rapid channel activation followed immediately by inactivation. However, even under normal conditions, a small late component of INa (INa,L) persists because of incomplete/failed inactivation of a subpopulation of channels. Notably, INa,L is directly linked with both congenital and acquired disease states. The multifunctional Ca(2+)/calmodulin-dependent kinase II (CaMKII) has been identified as an important activator of INa,L in disease. Several potential CaMKII phosphorylation sites have been discovered, including Ser571 in the Nav1.5 DI-DII linker, but the molecular mechanism underlying CaMKII-dependent regulation of INa,L in vivo remains unknown.

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