9FJG

Two PLK1 PBD proteins bound to CENP-U(58-114) phosphorylated at Thr98

Summary for 9FJG

• Entry DOI: 10.2210/pdb9fjg/pdb
• Descriptor: Serine/threonine-protein kinase PLK1, Centromere protein U, TETRAETHYLENE GLYCOL, ... (6 entities in total)
• Functional Keywords: plk1, pbd, cell cycle, ccan, kinase, mitosis, kinetochore, cenp-u, phosphorylation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 67490.04

Authors

Ren, L.,Gasper, R.,Vetter, I.R.,Musacchio, A. (deposition date: 2024-05-31, release date: 2025-09-24, Last modification date: 2026-10-07)

Primary citation

Ren, L.,Esposito-Verza, A.,Gasper, R.,Pesenti, M.E.,Janning, P.,Muller, F.,Koerner, C.,Geue, P.,Wohlgemuth, S.,Vetter, I.R.,Musacchio, A.
Molecular anatomy of PLK1 master docking motifs.
Nat Commun, 17:-, 2026

PubMed Abstract: The Polo-box domain (PBD) localizes Polo-like kinase 1 (PLK1) near mitotic substrates required for chromosome biorientation. Recent work on mitotic kinetochores showed PLK1 docking begins hierarchically at master docking motifs on BUB1 and CENP-U. Whether master docking motifs have common molecular features remains poorly understood. Presence on CENP-U of two neighbouring motifs generated by initial CDK1 priming and subsequent PLK1 phosphorylation led us to hypothesize PBD dimerization might be involved. Using biochemical, biophysical, and modelling approaches, we gathered strong evidence that CENP-U contains a single master docking motif. The motif is very high affinity and sufficient to form extensive interactions with the PBD, engaging multiple pockets on its surface without obvious added benefits from dimerization. Comparisons with motifs in BUB1, BUBR1, and PRC1 suggest commonalities of master PLK1 docking motifs. We discuss the implications of our observations for the mechanism of PLK1 activation.

PubMed: 42115593
DOI: 10.1038/s41467-026-73038-8

Experimental method

X-RAY DIFFRACTION (2 Å)