![Sample our Bioscience journals, sign in here to start your access, Latest two full volumes FREE to you for 14 days]({"type":"image" , "src" : "/sda/5925/TOC-Subject-Sample-2021-Bioscience.jpg"})
Abstract
ZO-1 (Zona Occludens protein 1) has previously been shown to bind Cx43α1. This interaction involves the most C-terminal residues of Cx43α1 and the second PDZ-domain of ZO-1. The biological significance of this interaction is not well understood. The similarity of the C-terminal residues of the lens connexins Cx46α3 and Cx50α8 to Cx43α1 prompted us to examine if ZO-1 is expressed in the lens, and if ZO-1 interacts with lens connexins. A high level of ZO-1 expression was detected in the mouse lens. Lens connexins were shown to co-immunoprecipitate with ZO-1, and the interaction was found to involve similar domains as those previously demonstrated for the Cx43α1/ZO-1 interaction (Nielsen et al. manuscript in preparation). Futhermore, transient expression of Cx46α3 and Cx50α8 in cell culture showed colocalization of gap junction plaques with ZO-1, further suggesting that lens connexins interact with ZO-1. Sequence comparison suggests that a large number of connexins of the alpha subclass may interact with ZO-1. Using the lens as a system to study connexin/ZO-1 interactions may further our understanding of their biological significance in the lens, as well as in other organs.
Key Words: