Role of protein kinase PLK1 in the epigenetic maintenance of centromeres.

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Bibliographic Details
Title: Role of protein kinase PLK1 in the epigenetic maintenance of centromeres.
Authors: Conti, Duccio, Verza, Arianna Esposito, Pesenti, Marion E., Cmentowski, Verena, Vetter, Ingrid R., Dongqing Pan, Musacchio, Andrea
Source: Science (pre-March 2025). 9/6/2024, Vol. 385 Issue 6713, p1091-1097. 7p. 4 Diagrams.
Subjects: Protein kinases, Cyclin-dependent kinases, Cell cycle, Cell physiology, Epigenetics
Abstract: The centromere, a chromosome locus defined by the histone H3-like protein centromeric protein A (CENP-A), promotes assembly of the kinetochore to bind microtubules during cell division. Centromere maintenance requires CENP-A to be actively replenished by dedicated protein machinery in the early G1 phase of the cell cycle to compensate for its dilution after DNA replication. Cyclin-dependent kinases (CDKs) limit CENP-A deposition to once per cell cycle and function as negative regulators outside of early G1. Antithetically, Polo-like kinase 1 (PLK1) promotes CENP-A deposition in early G1, but the molecular details of this process are still unknown. We reveal here a phosphorylation network that recruits PLK1 to the deposition machinery to control a conformational switch required for licensing the CENP-A deposition reaction. Our findings clarify how PLK1 contributes to the epigenetic maintenance of centromeres. [ABSTRACT FROM AUTHOR]
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Database: Psychology and Behavioral Sciences Collection
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Abstract:The centromere, a chromosome locus defined by the histone H3-like protein centromeric protein A (CENP-A), promotes assembly of the kinetochore to bind microtubules during cell division. Centromere maintenance requires CENP-A to be actively replenished by dedicated protein machinery in the early G1 phase of the cell cycle to compensate for its dilution after DNA replication. Cyclin-dependent kinases (CDKs) limit CENP-A deposition to once per cell cycle and function as negative regulators outside of early G1. Antithetically, Polo-like kinase 1 (PLK1) promotes CENP-A deposition in early G1, but the molecular details of this process are still unknown. We reveal here a phosphorylation network that recruits PLK1 to the deposition machinery to control a conformational switch required for licensing the CENP-A deposition reaction. Our findings clarify how PLK1 contributes to the epigenetic maintenance of centromeres. [ABSTRACT FROM AUTHOR]
ISSN:00368075
DOI:10.1126/science.ado5178