During recent years, the bioluminescence resonance energy transfer (BRET) methodology has emerged as a powerful technique for the study of protein-protein interactions. This review focuses on recent work demonstrating the power of BRET for the study of tyrosine kinase receptors, using insulin and IGF-1 receptors as models. The authors show that BRET can be used to monitor ligand-induced conformational changes within homodimeric insulin and IGF-1 receptors, as well as heterodimeric insulin/IGF-1 hybrid receptors. BRET can also be used to study, in real time and in living cells, the interaction of tyrosine kinase receptors with cellular partners negatively or positively involved in the regulation of intracellular signalling (protein tyrosine phosphatases, molecular adaptors). In addition, BRET can be used to develop high-throughput screening assays for the search of molecules with therapeutic interest and could, therefore, constitute a valuable tool for laboratories involved in drug discovery.