Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis
Novo Nordisk Foundation · Max Planck Institute of Biochemistry · +5 more institutions
Abstract
Eukaryotic cells replicate by a complex series of evolutionarily conserved events that are tightly regulated at defined stages of the cell division cycle. Progression through this cycle involves a large number of dedicated protein complexes and signaling pathways, and deregulation of this process is implicated in tumorigenesis. We applied high-resolution mass spectrometry-based proteomics to investigate the proteome and phosphoproteome of the human cell cycle on a global scale and quantified 6027 proteins and 20,443 unique phosphorylation sites and their dynamics. Co-regulated proteins and phosphorylation sites were grouped according to their cell cycle kinetics and compared to publicly available messenger RNA…
Citation impact
- FWCI
- 68.29
- Percentile
- 100%
- References
- 62
Authors
12- JVJesper V. OlsenCorresponding
Novo Nordisk Foundation, Max Planck Institute of Biochemistry
- MVMichiel VermeulenCorresponding
Cancer Genomics Centre, Max Planck Institute of Biochemistry
- ASAnna SantamaríaCorresponding
University of Basel
- CKChanchal KumarCorresponding
Experimental Drug Development Centre, Max Planck Institute of Biochemistry
- MLMartin L. Miller
Memorial Sloan Kettering Cancer Center, Novo Nordisk Foundation
Topics & keywords
- Phosphoproteomics
- Mitosis
- Phosphorylation
- Cell biology
- Occupancy
- Biology
- Computational biology
- Protein phosphorylation