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Basolateral targeting by leucine‐rich repeat domains in epithelial cells
Author(s) -
Legouis Renaud,
JaulinBastard Fanny,
Schott Sonia,
Navarro Christel,
Borg JeanPaul,
Labouesse Michel
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400006
Subject(s) - pdz domain , epithelial polarity , caenorhabditis elegans , microbiology and biotechnology , cell polarity , leucine rich repeat , biology , polarity (international relations) , membrane protein , subcellular localization , apical membrane , protein domain , transport protein , cell , epithelium , biochemistry , genetics , cytoplasm , gene , membrane , kinase
The asymmetric distribution of proteins to basolateral and apical membranes is an important feature of epithelial cell polarity. To investigate how basolateral LAP proteins (LRR (for leucine‐rich repeats) and PDZ (for PSD‐95/Discs‐large/ZO‐1), which play key roles in cell polarity, reach their target membrane, we carried out a structure–function study of three LAP proteins: Caenorhabditis elegans LET‐413, human Erbin and human Scribble (hScrib). Deletion and point mutation analyses establish that their LRR domain is crucial for basolateral membrane targeting. This property is specific to the LRR domain of LAP proteins, as the non‐LAP protein SUR‐8 does not localize at the basolateral membrane of epithelial cells, despite having a closely related LRR domain. Importantly, functional studies of LET‐413 in C. elegans show that although its PDZ domain is dispensable during embryogenesis, its LRR domain is essential. Our data establish a novel paradigm for protein localization by showing that a subset of LRR domains direct subcellular localization in polarized cells.