The vertebrate adhesive junction proteins β-catenin and plakoglobin and the Drosophila segment polarity gene armadillo form a multigene family with similar properties

Mark Peifer, Pierre D. McCrea, Kathleen J. Green, Eric Wieschaus, Barry M. Gumbiner

Research output: Contribution to journalArticle

284 Scopus citations

Abstract

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 β-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 β-catenin. Using anti-armadillo and antiplakoglobin antibodies, it was shown that β-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 β-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 β-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.

Original languageEnglish (US)
Pages (from-to)681-691
Number of pages11
JournalJournal of Cell Biology
Volume118
Issue number3
DOIs
StatePublished - Aug 1992

All Science Journal Classification (ASJC) codes

  • Cell Biology

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