title: Connexin43 regulates sodium current; ankyrin-G modulates gap junctions: the intercalated disc exchanger.
abstract: Intercalated disc structures have conventionally been considered to be independent. Recent work shows that molecules initially thought of as belonging to one complex can actually affect another. Here, I focus on the cross-talk between connexin43 (Cx43, 'the gap junction protein') and the sodium channel complex and, conversely, on ankyrin-G (AnkG, a 'component of the sodium channel complex') and gap junctions. I speculate as to the possibility that one molecule affects the function of the other by regulating its trafficking into the intercalated disc.
authors.forename: Mario
authors.initials: M
authors.lastname: Delmar
mesh_terms: D017487:Ankyrins / Q000502:physiology*; D018031:Connexin 43 / Q000502:physiology*; D017629:Gap Junctions / Q000502:physiology*; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000502:physiology; D008870:Microtubules / Q000502:physiology; D015222:Sodium Channels / Q000502:physiology*
chemical_list: C490613:ANK3 protein, human; D017487:Ankyrins; D018031:Connexin 43; C500216:GJA1 protein, human; C500985:MAPRE1 protein, human; C403664:MAPRE3 protein, human; D008869:Microtubule-Associated Proteins; D015222:Sodium Channels