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Originally published as Biophys J. BioFAST on October 7, 2005.
doi:10.1529/biophysj.105.066373
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Biophysical Journal 90:140-150 (2006)
© 2006 The Biophysical Society

Conductance of Connexin Hemichannels Segregates with the First Transmembrane Segment

Xinge Hu, Meiyun Ma and Gerhard Dahl

Department of Physiology and Biophysics, University of Miami, School of Medicine, Miami, Florida 33101

Correspondence: Address reprint requests to Gerhard Dahl, University of Miami School of Medicine, Dept. of Physiology and Biophysics, 1600 NW 10th Ave., Miami, FL 33136. Tel.: 305-243-5776; Fax: 305-243-5931; E-mail: gdahl{at}miami.edu.

Gap junction channels are intercellular channels that mediate the gated transfer of molecules between adjacent cells. To identify the domain determining channel conductance, the first transmembrane segment (M1) was reciprocally exchanged between Cx46 and Cx32E143. The resulting chimeras exhibited conductances similar to that of the respective M1 donor. Furthermore, a chimera with the carboxy-terminal half of M1 in Cx46 replaced by that of Cx32 exhibited a conductance similar to that of Cx32E143, whereas the chimera with only the amino-terminal half of M1 replaced retained the unitary conductance of wild-type Cx46. Extending the M1 domain swapping to other connexins by replacing the carboxy-terminal half of M1 in Cx46 with that of Cx37 yielded a chimera channel with increased unitary conductance close to that of Cx37. Furthermore, a point mutant of Cx46, with leucine substituted by glycine in position 35, displayed a conductance much larger than that of the wild type. Thus, the M1 segment, especially the second half, contains important determinants of conductance of the connexin channel.




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