Adherens junctions mediate cell–cell adhesion in epithelia and are important for development, tissue homeostasis and cell polarity. α-Catenin provides the link between junctional cadherins and actin through its ability to associate with β-catenin – which can bind to the cytoplasmic tail of cadherins – as well as F-actin and F-actin-binding proteins. Controversy remains, however, about how α-catenin forms this link: one model proposes that it acts as a physical linker that remains associated with the cadherin–β-catenin complex, whereas another model suggests that α-catenin acts through an allosteric mechanism whereby it dissociates from β-catenin to subsequently form a homodimer that can interact with F-actin. In addition, recent evidence has suggested adhesion-independent cytoplasmic roles for α-catenin. Ulrich Tepass and colleagues (p. 233) now generate Drosophila α-Catenin (α-Cat) mutants to investigate which of the models represents cellular events in vivo. The α-Cat mutants exhibit developmental defects that are consistent with a loss of cadherin function, and DE-cadherin and Armadillo (β-catenin) are lost from cell contacts. Interestingly, the α-Cat mutant phenotype can be rescued by expressing a DE-cadherin::α-Catenin fusion protein, which suggests that – at least in the tissues tested – α-Catenin acts in association with DE-cadherin and does not have cadherin-independent cytoplasmic functions.