| Autor: |
Nielsen, Peter A., Baruch, Amos, Shestopalov, Valery I., Giepmans, Ben N.G., Dunia, Irene, Benedetti, E. Lucio, Kumar, Nalin M. |
| Zdroj: |
Molecular Biology of the Cell; June 2003, Vol. 14 Issue: 6 p2470-2481, 12p |
| Abstrakt: |
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. |
| Databáze: |
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