Structural bases for the chemical regulation of Connexin43 channels

Mario Delmar, Wanda Coombs, Paul Sorgen, Heather S. Duffy, Steven M. Taffet

Research output: Contribution to journalReview articlepeer-review

83 Scopus citations


Connexins proteins associate with a variety of catalytic and non-catalytic molecules. Also, different domains of connexin can bind to each other, providing a mechanism for channel regulation. Here, we review some of these associations, placing particular emphasis on the intramolecular interactions that regulate Connexin43 (Cx43). We also describe some novel methods that allow for the characterization of protein-protein interactions such as those observed in the cardiac gap junction protein Connexin43. Overall, intra- and inter-molecular interactions may regulate gap junctions to filter the passage of molecular messages between cells at the appropriate time and between the appropriate cells. As a potential area for future investigations, we also speculate as to whether some of the inter-molecular interactions involving connexins lead to modifications in the function of the associated protein, rather than on the function of connexin itself.

Original languageEnglish (US)
Pages (from-to)268-275
Number of pages8
JournalCardiovascular research
Issue number2
StatePublished - May 1 2004


  • Connexin
  • Cx43
  • Gap junction regulation
  • Gap junctions

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine
  • Physiology (medical)


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