Integrins are essential components of focal adhesions that link cells to the extracellular matrix (ECM). Intracellularly, these adhesion receptors associate with a dynamic network of proteins – the integrin adhesion complex (IAC). The cytosolic adaptor protein talin not only links integrins and the IAC, but also directly connects integrins with actin and regulates their affinity for the ECM. But how does talin carry out all of these roles? On page 1844, Guy Tanentzapf and colleagues now provide an answer. They find that the two integrin-binding sites (IBS-1 and IBS-2) on talin act redundantly to recruit the adaptor to the cytoplasmic integrin tail, and also carry out specific, differential roles that provide a regulatory mechanism for integrin-mediated adhesion. Whereas the IBS-2 domain is required to maintain the link between integrins and the IAC, the IBS-1 domain regulates integrin binding to ECM ligands through an inside-out activation mechanism. By replacing wild-type talin with proteins mutated in the IBS-1 or IBS-2 domains, Tanentzapf and co-workers also show that the two domains confer individual functions during Drosophila melanogaster development. These observations highlight a mechanism through which diversity in integrin-mediated adhesion can be achieved and suggest a regulatory switch in the talin –integrin interaction, with important roles during development.