Protein–protein interactions are traditionally assessed using glutathione S-transferase (GST) pulldowns or co-immunoprecipitations followed by electrophoresis and immunoblotting, or by yeast two-hybrid (Y2H) assays; however, these can lead to many false-positive and false-negative results. In this issue (p. 2351), Kazuhisa Nakayama and colleagues developed a novel visible immunoprecipitation (VIP) assay to study protein–protein interactions by using a conventional fluorescent microscope or microplate reader, but without the need for electrophoresis and immunoblotting. As a proof of principle, they used VIP here to study the architecture of two multiprotein complexes: the BBSome, which is involved in the transport of ciliary material, and the exocyst, which tethers exocytic vesicles to the plasma membrane. The authors confirmed previously reported interactions and also discovered new ones, for example between the exocyst subunits Sec3 and Sec6, thus elegantly delineating the full set of interactions of each complex. They were also able to visualise the hierarchy of binding for up to four BBSome subunits. Moreover, by sequentially subtracting specific subunits of the exocyst from the samples, they demonstrated that the VIP assay can also be used to uncover one-to-many protein interactions. Therefore, with its capabilities that go beyond those of co-immunoprecipitations or GST pulldowns, but without the caveats of Y2H assays, VIP has the potential to become the new benchmark amongst the assays that measure protein interactions.