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

Nat Cell Biol. 2003 Jul;5(7):619-25. doi: 10.1038/ncb1002.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

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

Substances

  • AJM-1 protein, C elegans
  • Cadherins
  • Caenorhabditis elegans Proteins
  • Claudin-1
  • Cytoskeletal Proteins
  • DNA, Complementary
  • Membrane Proteins
  • Trans-Activators
  • VAB-9 protein, C elegans
  • alpha Catenin
  • beta Catenin
  • hmr-1 protein, C elegans

Associated data

  • GENBANK/AY275709