E-Cadherin and APC Compete for the Interaction with β-Catenin and the Cytoskeleton

• Published in: The Journal of cell biology 1994-12, Vol.127 (6), p.2061-2069
• Main Authors: Hülsken, Jörg, Birchmeier, Walter, Behrens, Jürgen
• Format: Article
• Language: English
• Subjects: Adenomatous Polyposis Coli Protein; alpha Catenin; Amino Acid Sequence; Antibodies; Base Sequence; beta Catenin; Cadherins; Cadherins - genetics; Cadherins - isolation & purification; Cadherins - metabolism; Catenins; Cell adhesion; Cell lines; Cells; Cells, Cultured; Cellular biology; Complementary DNA; Cytoskeletal Proteins - genetics; Cytoskeletal Proteins - isolation & purification; Cytoskeletal Proteins - metabolism; Cytoskeleton - metabolism; Desmoplakins; Embryonic cells; Epithelial cells; Fluorescent Antibody Technique; gamma Catenin; Genes; Intercellular Junctions; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Neurons; Precipitin Tests; Protein Binding; Recombinant Proteins - metabolism; Trans-Activators; Tumors
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.127.6.2061

β-Catenin is involved in the formation of adherens junctions of mammalian epithelia. It interacts with the cell adhesion molecule E-cadherin and also with the tumor suppressor gene product APC, and the Drosophila homologue of β-catenin, armadillo, mediates morphogenetic signals. We demonstrate here that E-cadherin and APC directly compete for binding to the internal, armadillo-like repeats of β-catenin; the NH2-terminal domain of β-catenin mediates the interaction of the alternative E-cadherin and APC complexes to the cytoskeleton by binding to α-catenin. Plakoglobin (γ-catenin), which is structurally related to β-catenin, mediates identical interactions. We thus show that the APC tumor suppressor gene product forms strikingly similar associations as found in cell junctions and suggest that β-catenin and plakoglobin are central regulators of cell adhesion, cytoskeletal interaction, and tumor suppression.