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 PMID:38034351  

Site-specific phosphorylation of ZYG-1 regulates ZYG-1 stability and centrosome number.

Jeffrey C Medley | Rachel N Yim | Joseph DiPanni | Brandon Sebou | Blake Shaffou | Evan Cramer | Colin Wu | Megan Kabara | Mi Hye Song
iScience | 2023

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 in vitro and physically interacts with ZYG-1 in vivo. 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.

Pubmed ID: 38034351

Research resources used in this publication

Antibodies used in this publication

None found

Associated grants

  • Agency: NIH HHS, United States
    Id: P40 OD010440
  • Agency: NIGMS NIH HHS, United States
    Id: R15 GM147857

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

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