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A more recent version of this article appeared on June 1, 2003
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Submitted on October 8, 2002
Revised on January 20, 2003
Accepted on January 21, 2003
3Cx46 and 8Cx50 interact with Zonula Occludens Protein-1 (ZO-1)
1 Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA
2 Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA (present address: Celera Genomics, South San Francisco, California 94080, USA)
3 Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, Missouri 63110, USA (present address: Bascom Palmer Eye Institute, University of Miami School of Medicine, Miami, Florida 33136, USA)
4 Division of Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam, The Netherlands
5 Institut Jacques Monod, CNRS-Universités Paris 6-Paris 7, Paris, France
6 Department of Ophthalmology and Visual Sciences, University of Illinois at Chicago, Chicago, Illinois 60612, USA
* Corresponding author. E-mail address: nalin{at}uic.edu.
Connexin 
1Cx43 has previously been shown to bind to the PDZ-domain containing protein ZO-1. The similarity of the carboxyl termini of this connexin and the lens fiber connexins 3Cx46 and 8Cx50, suggested that these connexins may also interact with ZO-1. ZO-1 was shown to be highly expressed in mouse lenses. Co-localization of ZO-1 with 3Cx46 and 8Cx50 connexins in fiber cells was demonstrated by immunofluorescence and by fracture-labeling electron microscopy, but showed regional variations through the lens. ZO-1 was found to co-immunoprecipitate with 3Cx46 and 8Cx50, and pull-down experiments showed that the second PDZ domain of ZO-1 was involved in this interaction. Transiently expressed 3Cx46 and 8Cx50 connexins lacking the COOH-terminal residues did not bind to the second PDZ domain, but still formed structures resembling gap junctions by immunofluorescence. These results indicate that ZO-1 interacts with lens fiber connexins 3Cx46 and 8Cx50 in a manner similar to that previously described for 1Cx43. The spatial variation in the interaction of ZO-1 with lens gap junctions is intriguing and is suggestive of multiple, dynamic roles for this association.
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