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- W2033025216 abstract "Mammalian sodium channels are composed of four homologous domains (DI, DII, DIII and DIV). Each domain is composed of six helical transmembrane segments (S1-S6). Together, the folding of S5-S6 segments of all the domains form the pore domain (PD). The S1-S4 segments of each domain form the voltage sensor domain (VSD). Recently, mutations in the VSD of Nav channels have been linked to pathologies such as hypo- and normokalemic periodic paralysis and recently dilated cardiomyopathyGosselin-Badaroudine P., et al.,(2012): PlosONE, 7(5):e38331. Here we use the histidine scanning mutagenesis technique to investigate the role of the positively charged amino acids along the S4 segments of each domain. Detecting a proton current at hyperpolarized potentials indicates that the mutated residue is located in the gating charge transfer center of the protein. Also, proton transport implicates that the mutated residue moves across the gating charge transfer center during activation. Furthermore, a shift in the Q-V curve indicate that the mutated residue plays an important role in the stabilization of the S4 segment in its activated or resting position. The results lead to the creation of the first structural model of the VSDs of a mammalian sodium channel in its resting state. This structural model features hydrophobic septa of different dimensions. Indeed, the VSD of the fourth domain displays a hydrophobic septum much larger than the septa of the other domains. This difference of the VSD of the forth domain provides a rationale for its late onset in the activation sequence and the fact that no gating pore current have been uncovered in the VSD of DIV of mammalian sodium channels." @default.
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- W2033025216 date "2013-01-01" @default.
- W2033025216 modified "2023-09-28" @default.
- W2033025216 title "Investigating the Voltage Sensor Domains of Nav1.4, its Structural and Functional Properties via Histidine Scanning Mutagenesis" @default.
- W2033025216 doi "https://doi.org/10.1016/j.bpj.2012.11.759" @default.
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