Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains.

@article{Bouvier2009CharacterizationOT,
  title={Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains.},
  author={Denis Bouvier and Gaelle Spagnol and Sylvie Chenavas and Fabien Kieken and Heidi Vitrac and Sarah Brownell and Admir Kellezi and Vincent Forge and Paul L Sorgen},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 49},
  pages={34257-71}
}
Gap junctions are intercellular channels that allow the passage of ions, small molecules, and second messengers that are essential for the coordination of cellular function. They are formed by two hemichannels, each constituted by the oligomerization of six connexins (Cx). Among the 21 different human Cx isoforms, studies have suggested that in the heart, Cx40 and Cx43 can oligomerize to form heteromeric hemichannels. The mechanism of heteromeric channel regulation has not been clearly defined… CONTINUE READING