Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells.

Détails

ID Serval
serval:BIB_18945
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells.
Périodique
FEBS Letters
Auteur(s)
Kausalya P.J., Reichert M., Hunziker W.
ISSN
0014-5793
Statut éditorial
Publié
Date de publication
2001
Volume
505
Numéro
1
Pages
92-96
Langue
anglais
Notes
Publication types: Journal Article
Résumé
Zonula occludens protein 1 (ZO-1) is a cytosolic tight junction protein that tethers transmembrane proteins such as occludin, claudin and junctional adhesion molecule to the actin cytoskeleton. The interaction between ZO-1 and claudin or junctional adhesion molecule occurs via the amino-terminal PSD95/Dlg/ZO-1 (PDZ) domains in ZO-1. A yeast two-hybrid screen to search for proteins that interact with the PDZ domains of ZO-1 identified connexin (Cx) 45. Cx45 interacts with the PDZ domains of ZO-1 and ZO-3, but not ZO-2, via a short C-terminal PDZ binding motif (SVWI). In transfected epithelial Madin-Darby canine kidney cells, Cx45 co-localizes with endogenous ZO-1 at or near tight junctions and co-precipitation experiments show that Cx45 and ZO-1 directly interact. Inactivating the C-terminal PDZ-binding motif in Cx45 affects its co-precipitation and co-localization with ZO-1. The growing number of connexins (i.e. Cx43 and Cx45) that can associate with ZO proteins indicate that ZO proteins may play a more general role in organizing gap junctions and/or in recruiting signaling molecules that regulate intercellular communication.
Mots-clé
Animals, Binding Sites, Carrier Proteins/metabolism, Cell Polarity, Cells, Cultured, Connexins/genetics, Connexins/metabolism, Dogs, Epithelial Cells/metabolism, Gap Junctions/metabolism, Kidney/cytology, Kidney/metabolism, Membrane Proteins/metabolism, Mice, Mutation, Phosphoproteins/metabolism, Protein Structure, Tertiary, Transfection, Two-Hybrid System Techniques
Pubmed
Web of science
Open Access
Oui
Création de la notice
19/11/2007 13:13
Dernière modification de la notice
20/08/2019 13:49
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