Abstract
Gap junctions are ubiquitous throughout the body, being present in all but one human tissue. They are essential for many body functions including, fetal development, cardiac muscle contraction, and functional neural networks. Numerous pathologies, such as wound healing, ocular cataracts, and heart disease have been linked to Gap junctions. However, there is still much that is unknown regarding Gap junction regulation and internalization. We are looking at the structural changes in Gap junction models using a Cx26/Cx43 hybrid structure caused by phosphorylation, ubiquitylation, and interaction of key residues with regulatory proteins MAPK, PKC, and Nedd4-E3-Ub-ligase.
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