Abstract
Spindle bipolarity is critical for genomic integrity. As centrosome number often dictates bipolarity, tight control of centrosome assembly is vital for faithful cell division. The master centrosome regulator ZYG-1/Plk4 plays a pivotal role in this process. In C.elegans, casein kinase II (CK2) negatively regulates centrosome duplication by controlling centrosome-associated ZYG-1 levels. Here, we investigated CK2 as a regulator of ZYG-1 and its impact on centrosome assembly. We show that CK2 phosphorylates ZYG-1 invitro and physically interacts with ZYG-1 invivo. Depleting CK2 or blocking ZYG-1 phosphorylation at CK2 target sites leads to centrosome amplification. Non-phosphorylatable ZYG-1 mutants exhibit elevated ZYG-1 levels, leading to increased ZYG-1 and downstream factors at centrosomes, thus driving centrosome amplification. Moreover, inhibiting the 26S proteasome prevents degradation of the phospho-mimetic ZYG-1. Our findings suggest that CK2-dependent phosphorylation of ZYG-1 controls ZYG-1 levels via proteasomal degradation to limit centrosome number.
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