Premium
hScrib interacts with ZO‐2 at the cell–cell junctions of epithelial cells
Author(s) -
Métais Jean-Yves,
Navarro Christel,
Santoni Marie-Josée,
Audebert Stéphane,
Borg Jean-Paul
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.062
Subject(s) - pdz domain , microbiology and biotechnology , septate junctions , cell junction , epithelial polarity , tight junction , adherens junction , cell , membrane protein , cell polarity , chemistry , cell membrane , suppressor , cell–cell interaction , biology , cadherin , membrane , gene , biochemistry
In Drosophila , the tumor suppressor Scribble is localized at the septate junctions of epithelial cells. Its mammalian homologue, hScrib, is a basolateral protein likely associated to proteins of the cell–cell junctions. We report the direct interaction between hScrib and ZO‐2, a junction‐associated protein. This interaction relies on two PDZ domains of hScrib and on the C‐terminal motif of ZO‐2. Both proteins localise at cell–cell junctions of epithelial cells. A point mutation in the LRR of hScrib delocalises the protein from the plasma membrane and abrogates the interaction with ZO‐2 but not with βPIX. Tyrosine phosphorylation of hScrib does not impair the interaction with ZO‐2. We show a direct link between two junctional proteins that are down‐regulated during cancer progression.