TitleThe vertebrate adhesive junction proteins beta-catenin and plakoglobin and the Drosophila segment polarity gene armadillo form a multigene family with similar properties.
Publication TypeJournal Article
Year of Publication1992
AuthorsPeifer, M, McCrea, PD, Green, KJ, Wieschaus, E, Gumbiner, BM
JournalJ Cell Biol
Date Published1992 Aug
KeywordsAmino Acid Sequence, Animals, Armadillo Domain Proteins, beta Catenin, Cadherins, Cell Adhesion Molecules, Cell Line, Cross Reactions, Cytoskeletal Proteins, Desmoglein 1, Desmogleins, Desmoplakins, Drosophila, Drosophila Proteins, Electrophoresis, Polyacrylamide Gel, Fluorescent Antibody Technique, gamma Catenin, Humans, Intercellular Junctions, Mice, Molecular Sequence Data, Multigene Family, Proteins, Sequence Homology, Nucleic Acid, Trans-Activators, Transcription Factors

Three proteins identified by quite different criteria in three different systems, the Drosophila segment polarity gene armadillo, the human desmosomal protein plakoglobin, and the Xenopus E-cadherin-associated protein beta-catenin, share amino acid sequence similarity. These findings raise questions about the relationship among the three molecules and their roles in different cell-cell adhesive junctions. We have found that antibodies against the Drosophila segment polarity gene armadillo cross react with a conserved vertebrate protein. This protein is membrane associated, probably via its interaction with a cadherin-like molecule. This cross-reacting protein is the cadherin-associated protein beta-catenin. Using anti-armadillo and antiplakoglobin antibodies, it was shown that beta-catenin and plakoglobin are distinct molecules, which can coexist in the same cell type. Plakoglobin interacts with the desmosomal glycoprotein desmoglein I, and weakly with E-cadherin. Although beta-catenin interacts tightly with E-cadherin, it does not seem to be associated with either desmoglein I or with isolated desmosomes. Anti-armadillo antibodies have been further used to determine the intracellular localization of beta-catenin, and to examine its tissue distribution. The implications of these results for the structure and function of different cell-cell adhesive junctions are discussed.

Alternate JournalJ. Cell Biol.