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. 2016 Jan 14;6:314. doi: 10.3389/fphar.2015.00314

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Copyright © 2016 Loussouarn, Sternberg, Nicole, Marionneau, Le Bouffant, Toumaniantz, Barc, Malak, Fressart, Péréon, Baró and Charpentier.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) Schematic representation of the localization of the binding sites of associated/regulatory proteins identified for Nav1.4 (blue), Nav1.5 (pink), or both (purple). Nav1.4 interaction with ankyrin is only suggested by chimeric constructs, it remains to be studied with full length proteins (Lemaillet et al., 2003). DI to DIV, domains I to IV; ID, intracellular interdomains; N-ter and C-ter, N-and C-terminus ends. (B) Table presenting the amino-acid (aa) numbering and length of specific regions and domains in Nav1.4 and Nav1.5 proteins. It is noticeable that Nav1.4 IDI-II total amino-acid length is shorter than Nav1.5 IDI-II.