Structural bases for the chemical regulation of Connexin43 channels.
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.
Delmar
Mario
M
Department of Pharmacology, SUNY Upstate Medical University, 766 Irving Ave, Syracuse, NY 13210, USA. delmarm@upstate.edu
Coombs
Wanda
W
Sorgen
Paul
P
Duffy
Heather S
HS
Taffet
Steven M
SM
D000818:Animals; D002450:Cell Communication; D002463:Cell Membrane Permeability; D018031:Connexin 43 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017629:Gap Junctions / Q000378:metabolism*; D005786:Gene Expression Regulation; D006801:Humans; D006863:Hydrogen-Ion Concentration; D015640:Ion Channel Gating; D009206:Myocardium / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D018031:Connexin 43