PLK2 phosphorylation is critical for CPAP function in procentriole formation during the centrosome cycle.

ABSTRACT: Control of centrosome duplication is tightly linked with the progression of the cell cycle. Recent studies suggest that the fundamental process of centriole duplication is evolutionally conserved. Here, we identified centrosomal P4.1-associated protein (CPAP), a human homologue of SAS-4, as a substrate of PLK2 whose activity oscillates during the cell cycle. PLK2 phosphorylates the S589 and S595 residues of CPAP in vitro and in vivo. This phosphorylation is critical for procentriole formation during the centrosome cycle. PLK4 also phosphorylates S595 of CPAP, but PLK4 phosphorylation is not a critical step in the PLK4 function in procentriole assembly. CPAP is phosphorylated in a cell cycle stage-specific manner, so that its phosphorylation increases at the G1/S transition phase and decrea

SUBMITTER: Chang J 

PROVIDER: S-EPMC2910268 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature