High resolution profiling of cell cycle-dependent protein and phosphorylation abundance changes in non-transformed cells.
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Authors
Rega, C
Tsitsa, I
Roumeliotis, TI
Krystkowiak, I
Portillo, M
Yu, L
Vorhauser, J
Pines, J
Mansfeld, J
Choudhary, J
Davey, NE
Tsitsa, I
Roumeliotis, TI
Krystkowiak, I
Portillo, M
Yu, L
Vorhauser, J
Pines, J
Mansfeld, J
Choudhary, J
Davey, NE
Document Type
Journal Article
Date
2025-03-16
Date Accepted
2025-02-24
Abstract
The cell cycle governs a precise series of molecular events, regulated by coordinated changes in protein and phosphorylation abundance, that culminates in the generation of two daughter cells. Here, we present a proteomic and phosphoproteomic analysis of the human cell cycle in hTERT-RPE-1 cells using deep quantitative mass spectrometry by isobaric labelling. By analysing non-transformed cells and improving the temporal resolution and coverage of key cell cycle regulators, we present a dataset of cell cycle-dependent protein and phosphorylation site oscillation that offers a foundational reference for investigating cell cycle regulation. These data reveal regulatory intricacies including proteins and phosphorylation sites exhibiting cell cycle-dependent oscillation, and proteins targeted for degradation during mitotic exit. Integrated with complementary resources, our data link cycle-dependent abundance dynamics to functional changes and are accessible through the Cell Cycle database (CCdb), an interactive web-based resource for the cell cycle community.
Citation
Nature Communications, 2025, 16 (1), pp. 2579 -
Source Title
Nature Communications
Publisher
NATURE PORTFOLIO
ISSN
2041-1723
eISSN
2041-1723
Collections
Research Team
Functional Proteomics
Directorate Cell & MolBio
Post-transl modification
Prote & Metabolomics Fac
Short Linear Motif
Directorate Cell & MolBio
Post-transl modification
Prote & Metabolomics Fac
Short Linear Motif