Site-Specific Phosphorylation of ZYG-1 Regulates ZYG-1 Stability and Centrosome Number.

ABSTRACT: Spindle bipolarity is critical for genomic integrity. Given that centrosome number often dictates mitotic bipolarity, tight control of centrosome assembly is vital for the fidelity of cell division. The kinase ZYG-1/Plk4 is a master centrosome factor that is integral for controlling centrosome number and is modulated by protein phosphorylation. While autophosphorylation of Plk4 has been extensively studied in other systems, the mechanism of ZYG-1 phosphorylation in C. elegans remains largely unexplored. In C. elegans, Casein Kinase II (CK2) negatively regulates centrosome duplication by controlling centrosome-associated ZYG-1 levels. In this study, we investigated ZYG-1 as a potential substrate of CK2 and the functional impact of ZYG-1 phosphorylation on centrosome assembly.

SUBMITTER: Medley JC 

PROVIDER: S-EPMC10274923 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature