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- W1988600868 abstract "Functional eukaryotic Na+ channels are composed of a single monomer with four homologous domains (DI-DIV), each with six transmembrane segments (S1-S6). In each domain, the fourth segment, S4, contains positive charges that transduce changes in voltage into channel gating. Previously, voltage clamp fluorometry (VCF) was applied to track the S4 voltage sensors in the rat muscle sodium channel, rNaV1.4 (Cha et al, Neuron, 1999 22(1):73-87). Our aim was to apply a similar methodology to the human cardiac sodium channel, hNaV1.5, which initiates the cardiac action potential, is the target of numerous anti-arrhythmic drugs and carries >100 mutations that are linked to inherited cardiac diseases. VCF reports on protein motion via an extracellular cysteine that is conjugated with a small fluorescent molecule, in our case tetramethylrhodamine maleimide. Within the extracellular S4 of each NaV1.5 domain, we have identified positions for cysteine substitutions that, when fluorescently tagged, display a voltage-sensitive change in fluorescence. Consistent with motions previously identified in rNaV1.4, and reflecting the role of each domain in gating, initial results show ultra-rapid outward movement of the S4 segments in DI, DII and DIII correlating with activation, but much slower translocation of the DIV S4 that is closer to the time scale of inactivation." @default.
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- W1988600868 date "2013-01-01" @default.
- W1988600868 modified "2023-09-28" @default.
- W1988600868 title "Applying Voltage Clamp Fluorometry to Track SCN5A Voltage Sensor Movement" @default.
- W1988600868 doi "https://doi.org/10.1016/j.bpj.2012.11.785" @default.
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