Marion E. Pesenti

The paper identifies a high-affinity master docking motif on CENP-U that interacts extensively with PLK1's Polo-box domain, suggesting common features among master PLK1 docking motifs.

This study identifies Bora as essential for Aurora A-mediated phosphorylation of PLK1's Thr210, revealing a unique interaction required for this process.

This study identifies multiple CCAN binding sites and shows that FACT localization to kinetochores depends on specific CCAN subcomplexes and is regulated by CK2 phosphorylation and DNA displacement.

The paper identifies a phosphorylation network regulated by PLK1 that controls a conformational switch necessary for CENP-A deposition, essential for centromere maintenance.