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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-08

AUTHORS

Cheng Tang, Xi Zhou, Yunxiao Zhang, Zhaohua Xiao, Zhaotun Hu, Changxin Zhang, Ying Huang, Bo Chen, Zhonghua Liu, Songping 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. More... »

PAGES

9241

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep09241

DOI

http://dx.doi.org/10.1038/srep09241

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014759607

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25784299


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