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The persistent current (I NaP ) through voltage-gated sodium channels enhances neuronal excitability by causing prolonged depolarization of membranes. Na v 1.3 intrinsically generates a small I NaP , although the mechanism underlying its generation remains unclear. In this study, the involvement of the four domains of Na v 1.3 in I NaP  generation was investigated using the tarantula toxin α-hexatoxin-MrVII (RTX-VII). RTX-VII activated Na v 1.3 and induced a large I NaP . A pre-activated state binding model was proposed to explain the kinetics of toxin-channel interaction. Of the four domains of Na v 1.3, both domain II and IV might play important roles in the toxin-induced I NaP . 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 I NaP  in Na v 1.3.

Synergetic Action of Domain II and IV Underlies Persistent Current Generation in Nav1.3 as revealed by a tarantula toxin