期刊
CARDIOVASCULAR RESEARCH
卷 93, 期 2, 页码 220-222出版社
OXFORD UNIV PRESS
DOI: 10.1093/cvr/cvr343
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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.
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