Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis
J. V. Olsen, M. Vermeulen, A. Santamaría, Chanchal Kumar, Martin L. Miller, L. Jensen, Florian Gnad, J. Cox, T. S. Jensen, E. Nigg, S. Brunak, M. Mann
2010.1.12Science Signaling
tlooto Summary
High-resolution mass spectrometry–based proteomics was applied 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, finding that nuclear proteins and proteins involved in regulating metabolic processes have high phosphorylated site occupancy in mitosis, suggesting that these proteins may be inactivated by phosphorylate in mitotic cells.
Abstract
Protein phosphorylation during the cell cycle may be an all-or-none process in many instances.
Citation format
OLSEN, J. V., et al. Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Science Signaling, 2010, 3: ra3-ra3.