PXD053933 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Mass spectrometry analysis of in vitro PLK1 phosphorylation |
Description | Polo-like kinase 1 (PLK1) protects against genome instability by ensuring timely and accurate mitotic cell division, and its activity is tightly regulated throughout the cell cycle. Although the pathways that initially activate PLK1 in G2 are well-characterized, the factors that directly regulate PLK1 in mitosis remain poorly understood. Here, we identify that human PLK1 activity is sustained by the DNA damage response kinase Checkpoint kinase 2 (Chk2) in mitosis. Chk2 directly phosphorylates PLK1 T210, a residue on its T-loop whose phosphorylation is essential for full PLK1 kinase activity. Loss of Chk2-dependent PLK1 activity causes increased mitotic errors, including chromosome misalignment, chromosome missegregation, and cytokinetic defects. Moreover, Chk2 deficiency increases sensitivity to PLK1 inhibitors, suggesting that Chk2 status may be an informative biomarker for PLK1 inhibitor efficacy. This work demonstrates that Chk2 sustains mitotic PLK1 activity and protects genome stability through discrete functions in interphase DNA damage repair and mitotic chromosome segregation. |
HostingRepository | PRIDE |
AnnounceDate | 2024-11-01 |
AnnouncementXML | Submission_2024-11-01_08:37:07.830.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Wenxue Li |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | phosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-07-13 16:43:55 | ID requested | |
⏵ 1 | 2024-11-01 08:37:08 | announced | |
Publication List
Black EM, Ram, í, rez Parrado CA, Trier I, Li W, Joo YK, Pichurin J, Liu Y, Kabeche L, Chk2 sustains PLK1 activity in mitosis to ensure proper chromosome segregation. bioRxiv, ():(2024) [pubmed] |
10.1101/2024.03.08.584115; |
Keyword List
submitter keyword: kinase, PRM, phosphorylation |
Contact List
Yansheng Liu |
contact affiliation | Yale Cancer Biology Institute |
contact email | yansheng.liu@yale.edu |
lab head | |
Wenxue Li |
contact affiliation | Yale University |
contact email | wenxue.li@yale.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD053933
- Label: PRIDE project
- Name: Mass spectrometry analysis of in vitro PLK1 phosphorylation