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Originally published as MBC in Press, 10.1091/mbc.E02-10-0637 on March 7, 2003

Vol. 14, Issue 6, 2470-2481, June 2003

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Lens Connexins {alpha}3Cx46 and {alpha}8Cx50 Interact with Zonula Occludens Protein-1 (ZO-1)

Peter A. Nielsen *, Amos Baruch * ¶, Valery I. Shestopalov {dagger} #, Ben N.G. Giepmans {ddagger}, Irene Dunia §, E. Lucio Benedetti §, and Nalin M. Kumar || **

* Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA; {dagger} Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, Missouri 63110, USA; {ddagger} Division of Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam, The Netherlands; § Institut Jacques Monod, CNRS-Universités Paris 6-Paris 7, Paris, France; and || Department of Ophthalmology and Visual Sciences, University of Illinois at Chicago, Chicago, Illinois 60612, USA

Submitted October 8, 2002; Revised January 20, 2003; Accepted February 26, 2003
Monitoring Editor: Daniel Goodenough

Connexin {alpha}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 {alpha}3Cx46 and {alpha}8Cx50 suggested that these connexins may also interact with ZO-1. ZO-1 was shown to be highly expressed in mouse lenses. Colocalization of ZO-1 with {alpha}3Cx46 and {alpha}8Cx50 connexins in fiber cells was demonstrated by immunofluorescence and by fracture-labeling electron microscopy but showed regional variations throughout the lens. ZO-1 was found to coimmunoprecipitate with {alpha}3Cx46 and {alpha}8Cx50, and pull-down experiments showed that the second PDZ domain of ZO-1 was involved in this interaction. Transiently expressed {alpha}3Cx46 and {alpha}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 {alpha}3Cx46 and {alpha}8Cx50 in a manner similar to that previously described for {alpha}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.

Present addresses: Celera Genomics, South San Francisco, CA 94080

# Present addresses: Bascom Palmer Eye Institute, University of Miami School of Medicine, Miami, FL 33136

** Corresponding author. E-mail address: nalin{at}uic.edu.




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