Journal
CELL COMMUNICATION AND ADHESION
Volume 8, Issue 4-6, Pages 213-217Publisher
TAYLOR & FRANCIS LTD
DOI: 10.3109/15419060109080726
Keywords
connexin; gap junctions; lens; ZO-1
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Funding
- NATIONAL EYE INSTITUTE [R01EY011093, R01EY012142, R01EY013605] Funding Source: NIH RePORTER
- NEI NIH HHS [EY12142, EY13605, EY11093] Funding Source: Medline
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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 coimmunoprecipitate 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). Furthermore, 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.
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