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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

287 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

ASJC Scopus subject areas

  • Cell Biology

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