Although adhesion to extracellular structures is one of the most fundamental cell biological processes, the intracellular signals triggered by integrins, the most important receptors involved, are incompletely understood. Several recent reports indicate that signaling by beta(2) and beta(3) integrins in various cell types (neutrophils, macrophages, osteoclasts and platelets) use components of the signal transduction machinery of lymphocyte antigen receptors. Central to this immunoreceptor-like signaling is the phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters (such as DAP12 and the Fc receptor gamma-chain) by Src-family kinases and the concomitant recruitment of the Syk tyrosine kinase through its dual SH2 domains. These and other reports reveal an unexpected similarity between the signal-transduction mechanisms used by integrins and immune recognition receptors.