Journal
SCIENTIFIC REPORTS
Volume 5, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep09241
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Funding
- National Basic Research Program of China (973 Program) [2010CB529801, 2012CB22305]
- National Science Foundation Project [31370783, 31370817]
- Cooperative Innovation Center of Engineering and New Products for Developmental Biology of Hunan Province [20134486]
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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 alpha-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.
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