MassIVE MSV000101084

Partial Public PXD075442

Analysis of the phosphorylation situation of CENP-U

Description

Study of the reconstituted in vitro human PLK1:CENP-U complex with PBD fused N-terminally to maltose-binding-protein (MBPPBD) and residues 58-114 of CENP-U fused N-terminally to MBP (MBPCENP-U58-114). To phosphorylate T78 and T98 of MBPCENP-U58-114, we added catalytic amounts (typically 1:30 molar ratio) of active CDK1 and PLK1 kinase. Either 1) pre-phosphorylating MBPCENP-U58-114 with both kinases before adding MBPPBD for complex formation (pre-phosphorylation method); or 2) mixing MBPCENP-U58-114 and MBPPBD with both kinases for simultaneous phosphorylation and complex formation (co-mixing method) were tested. [doi:10.25345/C5QJ78C0F] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: phosphorylation ; proteomics ; CENP-U ; DatasetType:Proteomics

Contact

Principal Investigators:
(in alphabetical order)
Petra Janning, MPI of Molecular Physiology, Germany
Submitting User: janning

Publications

Long Ren, Arianna Esposito-Verza, Raphael Gasper, Marion E. Pesenti, Petra Janning, Franziska Müller, Carolin Koerner, Petra Geue, Sabine Wohlgemuth, Ingrid R. Vetter & Andrea Musacchio.
Molecular anatomy of PLK1 master docking motifs.
Nat Commun 17, 4228 (2026). https://doi.org/10.1038/s41467-026-73038-8.

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