Centrosomes not only function as microtubule organising centres, but are also essential for correct mitotic spindle assembly and cell cycle progression. Each cell contains a single centrosome, which is replicated precisely once per cell cycle, and a number of centriolar and PCM proteins have been implicated in the regulation of the centrosome duplication cycle. The nimA-related serine/threonine-protein kinase NEK7 also localises to the centrosome and is required for the correct formation of the mitotic spindle. But is this kinase also involved in centriole duplication? On page 3760, Kunsoo Rhee and colleagues now provide an answer to this question by showing that depletion of NEK7 by using siRNA inhibits centriole duplication. By contrast, the ectopic expression of a centrosome-targeted version of the kinase results in centriole overduplication. Furthermore, NEK7 is required for the specific recruitment of PCM proteins during interphase and depletion of the kinase results in centrosome maturation defects that, in turn, affect correct formation of the bipolar spindle. However, depletion of PLK4, which is known to be essential for centriole duplication, does not affect PCM accumulation. The researchers, therefore, conclude that NEK7 is essential for the recruitment of PCM to the centriole prior to its duplication, which then provides the correct environment for activation of PLK4 and the subsequent initiation of centriole duplication.