Abstract
Vertebrate gap junctions, composed of integral membrane proteins encoded by the connexin gene family, are critically important in regulation of embryonic development, coordinated contraction of excitable cells, tissue homeostasis, normal cell growth, and differentiation. Connexin proteins typically have short half-lives and detergent-specific solubilities, and interact with a variety of protein-binding partners during the assembly, trafficking, assembly/disassembly, and degradation of the oligomeric forms that constitute hemichannels and junctional channels. Phosphorylation has been implicated in the regulation of gap junctional communication at several stages of the connexin life cycle including hemichannel oligomerization, export of the protein to the plasma membrane, hemichannel activity, gap junction assembly, gap junction channel gating, and connexin degradation.
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