An Ala/Glu difference in E1 of Cx26 and Cx30 contributes to their differential anionic permeabilities.

ABSTRACT: Two closely related connexins, Cx26 and Cx30, share widespread expression in the cochlear cellular networks. Gap junction channels formed by these connexins have been shown to have different permeability profiles, with Cx30 showing a strongly reduced preference for anionic tracers. The pore-forming segment of the first extracellular loop, E1, identified by computational studies of the Cx26 crystal structure to form a parahelix and a narrowed region of the pore, differs at a single residue at position 49. Cx26 contains an Ala and Cx30, a charged Glu at this position, and cysteine scanning in hemichannels identified this position to be pore-lining. To assess whether the Ala/Glu difference affects permeability, we modeled and quantified Lucifer Yellow transfer between HeLa cell pairs expressi

SUBMITTER: Kraujaliene L 

PROVIDER: S-EPMC11415307 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature