Lens connexins α3Cx46 and α8Cx50 interact with zonula occludens protein-1 (ZO-1)

Peter A. Nielsen, Amos Baruch, Valery I. Shestopalov, Ben N.G. Giepmans, Irene Dunia, E. Lucio Benedetti, Nalin M. Kumar

Research output: Contribution to journalArticlepeer-review

91 Scopus citations


Connexin α1Cx43 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 α3Cx46 and α8Cx50 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 α3Cx46 and α8Cx50 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 α3Cx46 and α8Cx50, and pull-down experiments showed that the second PDZ domain of ZO-1 was involved in this interaction. Transiently expressed α3Cx46 and α8Cx50 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 α3Cx46 and α8Cx50 in a manner similar to that previously described for α1Cx43. 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.

Original languageEnglish (US)
Pages (from-to)2470-2481
Number of pages12
JournalMolecular biology of the cell
Issue number6
StatePublished - Jun 1 2003

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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