Connexin43 regulates sodium current; ankyrin-G modulates gap junctions: the intercalated disc exchanger.

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.