Cx30.2 can form heteromeric gap junction channels with other cardiac connexins.
Since most cells in the heart co-express multiple connexins, we studied the possible heteromeric interactions between connexin30.2 and connexin40, connexin43 or connexin45 in transfected cells. Double-label immunofluorescence microscopy showed that connexin30.2 extensively co-localized with each co-expressed connexin at appositional membranes. When Triton X-100 solubilized connexons were affinity purified from co-expressing cells, connexin30.2 was isolated together with connexin40, connexin43, or connexin45. Co-expression of connexin30.2 with connexin40, connexin43, or connexin45 did not significantly reduce total junctional conductance. Gap junction channels in cells co-expressing connexin30.2 with connexin43 or connexin45 exhibited voltage-dependent gating intermediate between that of either connexin alone. In contrast, connexin30.2 dominated the voltage-dependence when co-expressed with connexin40. Our data suggest that connexin30.2 can form heteromers with the other cardiac connexins and that mixed channel formation will influence the gating properties of gap junctions in cardiac regions that co-express these connexins.
Gemel
Joanna
J
University of Chicago, Department of Pediatrics MC 4060, 5841 S. Maryland Avenue, Chicago, IL 60637-1470, USA.
Lin
Xianming
X
Collins
Raymond
R
Veenstra
Richard D
RD
Beyer
Eric C
EC
D002460:Cell Line; D018031:Connexin 43 / Q000378:metabolism*; D017630:Connexins / Q000378:metabolism*; D017629:Gap Junctions / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007668:Kidney / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism*; D011485:Protein Binding; D000097003:Gap Junction alpha-5 Protein
D018031:Connexin 43; D017630:Connexins; D046912:Multiprotein Complexes; D000097003:Gap Junction alpha-5 Protein; C500216:GJA1 protein, human; C510757:connexin 30.2, mouse; C082920:connexin 45