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Papers In Press, published online ahead of print November 15, 2001
J. Biol. Chem, 10.1074/jbc.M109652200
Submitted on October 5, 2001
Revised on November 15, 2001
Accepted on November 15, 2001

Interaction between Erbin and a catenin-related protein in epithelial cells

Fanny Jaulin-Bastard, Jean-Pierre Arsanto, André Le Bivic, Christel ;Navarro, Frédéric Vély, Hiroko Saito, Sylvie Marchetto, Mechthild Hatzfeld, Marie-Josée Santoni, Daniel Birnbaum, and Jean-Paul Borg

Department of Molecular Oncology, INSERM U119, Marseille 13009

Corresponding Author: borg{at}marseille.inserm.fr

Integrity of epithelial tissues relies on the proper apical-basolateral polarity of epithelial cells. Members of the LAP (LRR and PDZ) protein family such as LET-413 and Scribble are involved in maintaining epithelial cell polarity in Caenorhabditis elegans and Drosophila melanogaster, respectively. We previously described Erbin as a mammalian LET-413 homologue interacting with ERBB2/HER2, an EGF receptor family member. Erbin and ERBB2/HER2 are located to the basolateral membranes of epithelial cells. We show here that Erbin interacts with p0071 (also called plakophilin-4), an armadillo-repeat protein linked to the cytoskeleton. Erbin binds to p0071 in vitro and in vivo in a PDZ domain dependent manner and both proteins colocalized in desmosomes of epithelial cells. Using a dominant-negative approach, we found that integrity of epithelial cell monolayer is impaired when interaction between Erbin and p0071 is disrupted. We propose that Erbin is connected by p0071 to cytoskeletal networks in an interaction crucial for epithelial homeostasis.


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