Author(s): Nielsen PA, Baruch A, Giepmans BN, Kumar NM
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Abstract ZO-1 (Zona Occludens protein 1) has previously been shown to bind Cx43alpha1. This interaction involves the most C-terminal residues of Cx43alpha1 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 Cx46alpha3 and Cx50alpha8 to Cx43alpha1 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 Cx43alpha1/ZO-1 interaction (Nielsen et al. manuscript in preparation). Futhermore, transient expression of Cx46alpha3 and Cx50alpha8 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.
This article was published in Cell Commun Adhes
and referenced in Journal of Clinical & Experimental Ophthalmology