Mother centrioles can be distinguished from their daughters by their competence to become basal bodies and to promote ciliary assembly, a capability conferred by the presence of appendages at their distal end. Distal appendages (DAs) are nanoscopic structures necessary for ciliary axoneme nucleation and for promoting ciliary vesicle docking. Thus, DAs confer key functional features enabling the centriole to basal body transition. Conceivably, DA protein components are not only essential for ciliogenesis but they are also mutated in a plethora of human ciliopathies. Recently, we and others established that DAs bear functions unrelated to ciliogenesis: in cycling cells, for instance, they also enable the centrosome to directly activate the p53 pathway via a signaling hub dubbed PIDDosome. Exploiting this advancement, I will discuss the generation of a novel fluorescent reporter capable of informing about the functional proficiency of DAs, both in flow cytometry and microscopy measurements. Our reporter can not only robustly respond to the presence/absence of functional DAs within a cell, but it is also sufficiently sensitive to highlight intermediate scenarios, such as those observed in the presence of hypomorphic mutations of the DA protein CEP83 found in nephronophthisis patients. Finally, I will show proof-of-concept data that our system is amenable to revealing both pharmacologic and genetic perturbation of DA functionality in high throughput screening settings. Given that a variety of human ciliopathies encompasses the reduction of DA functionality, our platform might be exploited to discover new ways to restore the proper ciliary functionality in ciliopathies.