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Journal Article

PLK1-mediated phosphorylation cascade activates Mis18 complex to ensure centromere inheritance

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Basquin,  Claire
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Parashara, P., Medina-Pritchard, B., Abad, M. A., Sotelo-Parrilla, P., Thamkachy, R., Grundei, D., et al. (2024). PLK1-mediated phosphorylation cascade activates Mis18 complex to ensure centromere inheritance. Science, 385(6713), 1098-1104. doi:10.1126/science.ado8270.


Cite as: https://hdl.handle.net/21.11116/0000-0010-34A7-7
Abstract
Accurate chromosome segregation requires the attachment of microtubules to centromeres, epigenetically defined by the enrichment of CENP-A nucleosomes. During DNA replication, CENP-A nucleosomes undergo dilution. To preserve centromere identity, correct amounts of CENP-A must be restored in a cell cycle-controlled manner orchestrated by the Mis18 complex (Mis18 alpha-Mis18 beta-Mis18BP1). We demonstrate here that PLK1 interacts with the Mis18 complex by recognizing self-primed phosphorylations of Mis18 alpha (Ser(54)) and Mis18BP1 (Thr(78) and Ser(93)) through its Polo-box domain. Disrupting these phosphorylations perturbed both centromere recruitment of the CENP-A chaperone HJURP and new CENP-A loading. Biochemical and functional analyses showed that phosphorylation of Mis18 alpha and PLK1 binding were required to activate Mis18 alpha-Mis18 beta and promote Mis18 complex-HJURP interaction. Thus, our study reveals key molecular events underpinning the licensing role of PLK1 in ensuring accurate centromere inheritance.