CEP120 and SPICE1 Cooperate with CPAP in Centriole Elongation

Centrosomes organize microtubule (MT) arrays and are comprised of centrioles surrounded by ordered pericentriolar proteins [1–4]. Centrioles are barrel-shaped structures composed of MTs, and as basal bodies they template the formation of cilia/flagella. Defects in centriole assembly can lead to ciliopathies and genome instability [5]. The assembly of procentrioles requires a set of conserved proteins [6–8]. It is initiated at the G1-to-S transition by PLK4 and CEP152 [9, 10], which help recruit SASS6 and STIL to the vicinity of the mother centriole to organize the cartwheel [11–14]. Subsequently, CPAP promotes centriolar MT assembly and elongation in G2 [15–17]. While centriole integrity is maintained by CEP135 and POC1 through MT stabilization [18–20], centriole elongation requires POC5 and is restricted by CP110 and CEP97 [21, 22]. How strict control of centriole length is achieved remains unclear. Here, we show that CEP120 and SPICE1 are required to localize CEP135 (but not SASS6, STIL, or CPAP) to procentrioles. CEP120 associates with SPICE1 and CPAP, and depletion of any of these proteins results in short procentrioles. Furthermore, CEP120 or CPAP overexpression results in excessive centriole elongation, a process dependent on CEP120, SPICE1, and CPAP. Our findings identify a shared function for these proteins in centriole length control. •CEP120 and SPICE1 functionally interact in centriole duplication and elongation•CEP120, SPICE1, and CPAP are required for CEP135 recruitment to procentrioles•CEP120 and SPICE1 are not required for SASS6, STIL, and CPAP recruitment•CEP120 and SPICE1 associate with CPAP and cooperate in centriole elongation