Specificity of the connexin W3/4 locus for functional gap junction formation.

ABSTRACT: The N-terminal (NT) domain of the connexins forms an essential transjunctional voltage (Vj) sensor and pore-forming domain that when truncated, tagged, or mutated often leads to formation of a nonfunctional channel. The NT domain is relatively conserved among the connexins though the α- and δ-group connexins possess a G2 residue not found in the β- and γ-group connexins. Deletion of the connexin40 G2 residue (Cx40G2Δ) affected the Vj gating, increased the single channel conductance (γj), and decreased the relative K(+)/Cl(-) permeability (PK/PCl) ratio of the Cx40 gap junction channel. The conserved α/β-group connexin D2/3 and W3/4 loci are postulated to anchor the NT domain within the pore via hydrophilic and hydrophobic interactions with adjacent connexin T5 and M34 residues. Cx40D3N and

SUBMITTER: Xu Q 

PROVIDER: S-EPMC5034775 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature