Synergetic action of domain II and IV underlies persistent current generation in Nav1.3 as revealed by a tarantula toxin

Scientific Reports
Cheng TangSongping Liang

Abstract

The persistent current (INaP) through voltage-gated sodium channels enhances neuronal excitability by causing prolonged depolarization of membranes. Nav1.3 intrinsically generates a small INaP, although the mechanism underlying its generation remains unclear. In this study, the involvement of the four domains of Nav1.3 in INaP generation was investigated using the tarantula toxin α-hexatoxin-MrVII (RTX-VII). RTX-VII activated Nav1.3 and induced a large INaP. A pre-activated state binding model was proposed to explain the kinetics of toxin-channel interaction. Of the four domains of Nav1.3, both domain II and IV might play important roles in the toxin-induced INaP. Domain IV constructed the binding site for RTX-VII, while domain II might not participate in interacting with RTX-VII but could determine the efficacy of RTX-VII. Our results based on the use of RTX-VII as a probe suggest that domain II and IV cooperatively contribute to the generation of INaP in Nav1.3.

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Citations

Jan 2, 2016·Toxicon : Official Journal of the International Society on Toxinology·Huai TaoSongping Liang
Feb 22, 2018·Annals of Neurology·Tariq ZamanEthan M Goldberg
Feb 26, 2019·The Journal of Biological Chemistry·Fan ZhangZhonghua Liu
Apr 13, 2017·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Cheng TangZhonghua Liu
Apr 25, 2018·Frontiers in Pharmacology·Xi ZhouZhonghua Liu

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