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Originally published In Press as doi:10.1074/jbc.M109652200 on November 15, 2001

J. Biol. Chem., Vol. 277, Issue 4, 2869-2875, January 25, 2002
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Interaction between Erbin and a Catenin-related Protein in Epithelial Cells*

Fanny Jaulin-Bastardab, Jean-Pierre Arsantoc, André Le Bivicc, Christel Navarroade, Frédéric Vélyf, Hiroko Saitoag, Sylvie Marchettoa, Mechthild Hatzfeldhi, Marie-Josée Santonia, Daniel Birnbauma, and Jean-Paul Borgadj

From the a U119 INSERM, Molecular Oncology, d Institut Paoli-Calmettes, Molecular Pharmacology, 27 boulevard Leï Roure 13009 Marseille, France, c IBDM, LGPD Faculté des Sciences de Luminy, case 907, 13288 Marseille cedex 09, France, f Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Université de la Méditerranée, Parc Scientifique de Luminy, case 906, 13288 Marseille cedex 09, France, and the h Molecular Biology Group, University of Halle, Magdeburger Strasse 18, 06097 Halle, Germany

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 epidermal growth factor receptor family member. Erbin and ERBB2/HER2 are located in 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.

* This project is supported by INSERM, ARC, La Ligue Nationale Contre le Cancer (Label Ligue), Fondation de France (to J.-P. B.) and Institute Paoli-Calmettes (to D. B. and J.-P. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

b Recipient of a Ministry of Research and Technology fellowship.

e Recipient of a Conseil Régional fellowship.

g Recipient of a Japanese-French fellowship.

i Supported by Deutsche Forschungsgemeinschaft grants Ha1791/3-3 and Ha1791/5-2 and the BMBF (Molecular Biology Group of Medical Faculty).

j To whom correspondence should be addressed: U119 INSERM, Molecular Oncology, 27 Blvd. Leï Roure 13009 Marseille, France. Tel.: 33-4-91-75-84-09; Fax: 33-4-91-26-03-64; E-mail: borg@marseille.inserm.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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