Signaling and adhesion activities of mammalian beta-catenin and plakoglobin in Drosophila.

The armadillo protein of Drosophila and its vertebrate homologues, beta-catenin and plakoglobin, are implicated in cell adhesion and wnt signaling. Here, we examine the conservation of these two functions by assaying the activities of mammalian beta-catenin and plakoglobin in Drosophila. We show that, in the female germ line, both mammalian beta-catenin and plakoglobin complement an armadillo mutation. We also show that shotgun mutant germ cells (which lack Drosophila E-cadherin) have a phenotype identical to that of armadillo mutant germ cells. It therefore appears that armadillo's role in the germ line is solely in a complex with Drosophila E-cadherin (possibly an adhesion complex), and both beta-catenin and plakoglobin can function in Drosophila cadherin complexes. In embryonic signaling assays, we find that plakoglobin has no detectable activity whereas beta-catenin's activity is weak. Surprisingly, when overexpressed, either in embryos or in wing imaginal disks, both beta-catenin and plakoglobin have dominant negative activity on signaling, an effect also obtained with COOH-terminally truncated armadillo. We suggest that the signaling complex, which has been shown by others to comprise armadillo and a member of the lymphocyte enhancer binding factor-1/T cell factor-family, may contain an additional factor that normally binds to the COOH-terminal region of armadillo.