Abstract
Epithelial cells are polarized, with apical and basal compartments demarcated by tight and adherens junctions. Proper establishment of these subapical junctions is critical for normal development and histogenesis. We report the characterization of the gene let-413 which has a critical role in assembling adherens junctions in Caenorhabditis elegans. In let-413 mutants, adherens junctions are abnormal and mislocalized to more basolateral positions, epithelial cell polarity is affected and the actin cytoskeleton is disorganized. The LET-413 protein contains one PDZ domain and 16 leucine-rich repeats with high homology to proteins known to interact with small GTPases. Strikingly, LET-413 localizes to the basolateral membrane. We suggest that LET-413 acts as an adaptor protein involved in polarizing protein trafficking in epithelial cells.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Caenorhabditis elegans / cytology*
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Caenorhabditis elegans / embryology*
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Caenorhabditis elegans / genetics
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Caenorhabditis elegans / metabolism
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Caenorhabditis elegans Proteins*
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Cell Adhesion
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Cell Membrane / chemistry
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Cell Membrane / metabolism
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Cell Polarity*
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Cytoskeleton / metabolism
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Cytoskeleton / ultrastructure
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Epithelial Cells / cytology*
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Epithelial Cells / metabolism
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Epithelial Cells / ultrastructure
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Epithelium / abnormalities
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Epithelium / metabolism
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Epithelium / ultrastructure
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Genes, Helminth / genetics
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Helminth Proteins / chemistry
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Helminth Proteins / genetics
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Helminth Proteins / metabolism*
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Intercellular Junctions / chemistry
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Intercellular Junctions / metabolism*
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Intercellular Junctions / ultrastructure
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Microscopy, Electron
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Molecular Sequence Data
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Mutation / genetics
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Phenotype
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Protein Structure, Tertiary
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Sequence Alignment
Substances
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Caenorhabditis elegans Proteins
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Helminth Proteins
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LET-413 protein, C elegans