CEP97 is a centrosomal protein that functions as a key negative regulator of ciliogenesis by capping the mother centriole and preventing cilia formation in collaboration with CP110 1. CEP97 is required for CP110 recruitment to the centrosome 1. Mechanistically, CEP97 does not directly bind microtubules but works with CP110 to control slow, processive microtubule elongation at centriolar distal ends 2. During ciliogenesis initiation, CEP97 must be removed from the mother centriole through ubiquitin-proteasome degradation via the cullin-3-RBX1-KCTD10 E3 ligase complex 3. CEP97 removal is facilitated by centriolar satellites and depends on Dyrk1a-mediated phosphorylation, which recruits Plk1 to promote centriole disengagement 45. Beyond ciliogenesis, CEP97 participates in aggresome assembly at the centrosome alongside CP110 and CEP290, supporting cellular proteostasis and aggregation of disease-relevant proteins like mutant huntingtin 6. CEP97 dysfunction contributes to ciliopathies through impaired ciliary assembly and trafficking 7. Glucocorticoid signaling regulates CEP97 expression in renal tubules, linking its function to kidney development 8. These findings establish CEP97 as a multifunctional regulator coordinating centriole dynamics, ciliogenesis, and protein quality control.