Structure-Function Study
We also investigate the fundamental structure-function relationship of gap junction channels organized by neuronal connexin (Cx36) and lens connexin (Cx50). We generated domain swapped chimeras and point mutations in these connexins to reveal the crucial domains/residues responsible for voltage-dependent gating (Vj-gating) and permeation efficiency at single channel levels. We also use homology modeling to investigate the structural basis of these functional properties.
Related Publications
- Tong, X., Aoyama, H., Tsukihara, T. and Bai, D.* (2014) Charge at the 46th residue of Cx50 is crucial for the gap junctional unitary conductance and transjunctional voltage-dependent gating. J Physiol 592, 5187-5202 [link to PubMed]
- Xin, L. and Bai, D.* (2013) Functional roles of the amino terminal domain in determining biophysical properties of Cx50 gap junction channels. Front Physiol 4, 373, 1-7 [link to PubMed]
- Xin, L., Sun, Y. and Bai, D.* (2012) Heterotypic connexin50/connexin50 mutant gap junction channels reveal interactions between two hemichannels during transjunctional voltage-dependent gating. J Physiol 590, 5037-5052 [link to PubMed]
