TY - JOUR T1 - A molecular mechanism for the procentriole recruitment of Ana2 JF - bioRxiv DO - 10.1101/647149 SP - 647149 AU - Tiffany A. McLamarrah AU - Sarah K. Speed AU - Daniel W. Buster AU - Carey J. Fagerstrom AU - Brian J. Galletta AU - Nasser M. Rusan AU - Gregory C. Rogers Y1 - 2019/01/01 UR - http://biorxiv.org/content/early/2019/05/23/647149.abstract N2 - Centriole duplication begins with the assembly of a pre-procentriole at a single site on a mother centriole and proceeds with the hierarchical recruitment of a conserved set of proteins, including Polo-like kinase 4 (Plk4)/ZYG-1, Ana2/SAS-5/STIL, and the cartwheel protein Sas6. During assembly, Ana2/STIL stimulates Plk4 kinase activity, and in turn, Ana2/STIL’s C-terminus is phosphorylated, allowing it to bind and recruit Sas6. The assembly steps immediately preceding Sas6-loading appear clear, but the mechanism underlying the upstream pre-procentriole recruitment of Ana2/STIL is not. In contrast to proposed models of Ana2/STIL recruitment, we recently showed that Drosophila Ana2 targets procentrioles independent of Plk4-binding. Instead, Ana2 recruitment requires Plk4 phosphorylation of Ana2’s N-terminus, but the mechanism explaining this process is unknown. Here, we show that the amyloid-like domain of Sas4, a centriole surface protein, binds Plk4 and Ana2, and facilitates phosphorylation of Ana2’s N-terminus which increases Ana2’s affinity for Sas4. Consequently, Ana2 accumulates at the procentriole to induce daughter centriole assembly. ER -