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

被引:77
|
作者
Jaulin-Bastard, F
Arsanto, JP
Le Bivic, A
Navarro, C
Vély, F
Saito, H
Marchetto, S
Hatzfeld, M
Santoni, MJ
Birnbaum, D
Borg, JP
机构
[1] INSERM U119, F-13009 Marseille, France
[2] Inst J Paoli I Calmettes, F-13009 Marseille, France
[3] Fac Sci Luminy, LGPD, IBDM, F-13288 Marseille, France
[4] Univ Mediterranee, CNRS, INSERM, Ctr Immunol Marseille Luminy, F-13288 Marseille 09, France
[5] Univ Halle Wittenberg, Mol Biol Grp, D-06097 Halle Saale, Germany
关键词
D O I
10.1074/jbc.M109652200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:2869 / 2875
页数:7
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