Ana1/Cep295 helps recruit Polo/PLK1 to centrioles to promote mitotic PCM assembly and centriole elongation
Polo kinase (PLK1) is a master cell cycle regulator that is recruited to various subcellular structures, often by its Polo-Box domain (PBD), which binds to phosphorylated S-pS/pT motifs. Polo/PLK1 has multiple functions at centrioles and centrosomes, and we previously showed that in Drosophila phosphorylated Sas-4 initiates Polo/PLK1 recruitment to newly formed centrioles, while phosphorylated Spd-2 recruits Polo/PLK1 to the Pericentriolar Material (PCM) that assembles around mother centrioles in mitosis. Here, we show that Ana1 (Cep295 in humans) also helps to recruit Polo to mother centrioles in Drosophila. If Ana1-dependent Polo/PLK1 recruitment is impaired, mother centrioles can still duplicate, disengage from their daughters and form functional cilia, but they can no longer efficiently assemble mitotic PCM or elongate during G2. We conclude that Ana1 helps recruit Polo/PLK1 to mother centrioles to specifically promote mitotic centrosome assembly and centriole elongation in G2, but not centriole duplication, centriole disengagement or cilia assembly.