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      The cell junction protein VAB-9 regulates adhesion and epidermal morphology in C. elegans.

      Nature cell biology

      beta Catenin, Actin Cytoskeleton, alpha Catenin, metabolism, Trans-Activators, Sequence Homology, Nucleic Acid, Sequence Homology, Amino Acid, genetics, Mutation, Molecular Sequence Data, Microscopy, Electron, isolation & purification, Membrane Proteins, ultrastructure, Intercellular Junctions, Epithelial Cells, Epidermis, analysis, DNA, Complementary, Cytoskeletal Proteins, Claudin-1, Cell Size, Cell Adhesion, Caenorhabditis elegans Proteins, Caenorhabditis elegans, Cadherins, Animals, Adherens Junctions

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          Abstract

          Epithelial cell junctions are essential for cell polarity, adhesion and morphogenesis. We have analysed VAB-9, a cell junction protein in Caenorhabditis elegans. VAB-9 is a predicted four-pass integral membrane protein that has greatest similarity to BCMP1 (brain cell membrane protein 1, a member of the PMP22/EMP/Claudin family of cell junction proteins) and localizes to the adherens junction domain of C. elegans apical junctions. Here, we show that VAB-9 requires HMR-1/cadherin for localization to the cell membrane, and both HMP-1/alpha-catenin and HMP-2/beta-catenin for maintaining its distribution at the cell junction. In vab-9 mutants, morphological defects correlate with disorganization of F-actin at the adherens junction; however, localization of the cadherin-catenin complex and epithelial polarity is normal. These results suggest that VAB-9 regulates interactions between the cytoskeleton and the adherens junction downstream of or parallel to alpha-catenin and/or beta-catenin. Mutations in vab-9 enhance adhesion defects through functional loss of the cell junction genes apical junction molecule 1 (ajm-1) and discs large 1 (dlg-1), suggesting that VAB-9 is involved in cell adhesion. Thus, VAB-9 represents the first characterized tetraspan adherens junction protein in C. elegans and defines a new family of such proteins in higher eukaryotes.

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          Author and article information

          Journal
          10.1038/ncb1002
          12819787

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