The Hydrophobic Residues in Amino Terminal Domains of Cx46 and Cx50 Are Important for Their Gap Junction Channel Ion Permeation and Gating.

ABSTRACT: Lens gap junctions (GJs) formed by Cx46 and Cx50 are important to keep lens transparency. Functional studies on Cx46 and Cx50 GJs showed that the V_j-gating, single channel conductance (γ_j), gating polarity, and/or channel open stability could be modified by the charged residues in the amino terminal (NT) domain. The role of hydrophobic residues in the NT on GJ properties is not clear. Crystal and cryo-EM GJ structures have been resolved, but the NT domain structure has either not been resolved or has showed very different orientations depending on the component connexins and possibly other experimental conditions, making it difficult to understand the structural basis of the NT in V_j-gating and γ_j. Here, we generated missense variants in Cx46 and

SUBMITTER: Jaradat R 

PROVIDER: S-EPMC9570504 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature