Summary a-catenin associates the cadherin-catenin complex with the actin cytoskeleton. a-catenin binds to b-catenin, which links it to the cadherin cytoplasmic tail, and F-actin, but also to a multitude of actin-associated proteins. These interactions suggest a highly complex cadherin-actin interface. Moreover, mammalian aE-catenin has been implicated in a cadherin-independent cytoplasmic function in Arp2/3-dependent actin regulation, and in cell signaling. The function and regulation of individual molecular interactions of a-catenin, in particular during development, are not well understood. We have generated mutations in Drosophila a-Catenin (a-Cat) to investigate a-Catenin function in this model, and to establish a setup for testing a-Catenin-related constructs in a-Cat-null mutant cells in vivo. Our analysis of a-Cat mutants in embryogenesis, imaginal discs and oogenesis reveals defects consistent with a loss of cadherin function. Compromising components of the Arp2/3 complex or its regulator SCAR ameliorate the a-Cat loss-of-function phenotype in embryos but not in ovaries, suggesting negative regulatory interactions between a-Catenin and the Arp2/3 complex in some tissues. We also show that the a-Cat mutant phenotype can be rescued by the expression of a DE-cadherin::a-Catenin fusion protein, which argues against an essential cytosolic, cadherin-independent role of Drosophila a-Catenin.