Role of protein kinase PLK1 in the epigenetic maintenance of centromeres

Author:

Conti Duccio1ORCID,Verza Arianna Esposito12,Pesenti Marion E.1ORCID,Cmentowski Verena12ORCID,Vetter Ingrid R.1ORCID,Pan Dongqing1ORCID,Musacchio Andrea12ORCID

Affiliation:

1. Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

2. Centre for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, 45141 Essen, Germany.

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 G 1 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 G 1 . Antithetically, Polo-like kinase 1 (PLK1) promotes CENP-A deposition in early G 1 , 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.

Publisher

American Association for the Advancement of Science (AAAS)

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