Polo-like kinase 4 (PLK4) is a key regulator of centriole biogenesis, but how PLK4 selects a single site for procentriole assembly remains unclear. Using ultrastructure expansion microscopy, we show that PLK4 localizes to discrete sites along the wall of parent centrioles. While there is variation in the number of sites PLK4 occupies on the parent centriole, most PLK4 localize at a dominant site that directs procentriole assembly. Inhibition of PLK4 activity leads to stable binding of PLK4 to the centriole and increases occupancy to a maximum of nine sites. We show that self-phosphorylation of an unstructured linker promotes the release of active PLK4 from the centriole to drive the selection of a single site for procentriole assembly. Preventing linker phosphorylation blocks PLK4 turnover, leading to supernumerary sites of PLK4 localization and centriole amplification. Therefore, self-phosphorylation is a major driver of the spatial patterning of PLK4 at the centriole and plays a critical role in selecting a single centriole duplication site.
PLK4 self-phosphorylation drives the selection of a single site for procentriole assembly
Disclosures: The authors declare no competing interests exist.
- Award Id(s): R01 GM133897,R01 GM114119,R01 CA266199
Phillip Scott, Ana Curinha, Colin Gliech, Andrew J. Holland; PLK4 self-phosphorylation drives the selection of a single site for procentriole assembly. J Cell Biol 4 December 2023; 222 (12): e202301069. doi: https://doi.org/10.1083/jcb.202301069
Download citation file: