Intercellular communication mediated by gap junctions plays an important role in a variety of cellular processes, including homeostasis, morphogenesis, cell differentiation, and regulation of growth.1–3 Gap junctions are transmembrane channels that directly link neighboring cells by regulating the exchange of low molecular weight (<1200D) metabolites, ions, and second messengers. Gap junctions are formed by the interaction of hemichannels (connexons) on adjacent cells. Each connexon is composed of a hexameric assembly of connexin proteins. Connexins are highly homologous proteins encoded by a multigene family with similar structural features, including a cytoplasmic N-terminal region, four transmembrane domains, two extracellular loops, and a C-terminal cytoplasmic tail. Comparison of the amino acid sequence of the various connexin family members indicates that the two areas of greatest divergence are the intracellular loop connecting the second and third transmembrane domains and the C-terminal tail.1–2 These distinct domains are thought to mediate connexin type-specific properties, including phosphorylation, responses to gating stimuli, and assembly and membrane turnover.
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