T-cell and B-cell antigen receptors are representative of a family of multisubunit receptors that utilize Src-family kinases as proximal cytoplasmic effectors in signal transduction. Recent studies have shown that distinct receptor subunits mediate ligand and effector interactions and demonstrate that physical interaction with effectors, and their activation, is a function of a 26 amino acid motif found in multiple receptor subunits. Further, receptor ligation induces tyrosine phosphorylation of this motif, and this initiates SH2-mediated association and activation of Src-family kinases and, apparently, ZAP70 kinases. Finally, this association triggers SH3-mediated binding of Lyn and Fyn to PI3-K, resulting in PI3-K activation. An integrated model of signal transduction is presented.