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Cardiovascular Research 2004 62(2):268-275; doi:10.1016/j.cardiores.2003.12.030
© 2004 by European Society of Cardiology
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Copyright © 2004, European Society of Cardiology

Structural bases for the chemical regulation of Connexin43 channels

Mario Delmar*,a, Wanda Coombsa, Paul Sorgenb, Heather S Duffyc and Steven M Taffetd

aDepartment of Pharmacology, SUNY Upstate Medical University, 766 Irving Ave, 13210 Syracuse, NY, USA
bDepartment of Biochemistry and Molecular Biology, University of Nebraska Medical Center. Omaha, NE, USA
cDepartment of Neuroscience, Albert Einstein College of Medicine, Bronx, NY, USA
dDepartment of Microbiology and Immunology, SUNY Upstate Medical University, Syracuse, NY, USA

* Corresponding author. Tel.: +1-315-464-7987; fax: +1-315-464-8014. Email address: delmarm{at}upstate.edu

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.

KEYWORDS Connexin; Gap junctions; Cx43; Gap junction regulation

Time for primary review 21 days


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