Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis

@article{Olsen2010QuantitativePR,
  title={Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis},
  author={Jesper V. Olsen and Michiel Vermeulen and Anna Santamaria and Chanchal Kumar and Martin L. Miller and Lars Juhl Jensen and Florian Gnad and J{\"u}rgen Cox and Thomas Sk{\o}t Jensen and Erich A. Nigg and S{\o}ren Brunak and Matthias Mann},
  journal={Science Signaling},
  year={2010},
  volume={3},
  pages={ra3 - ra3}
}
Protein phosphorylation during the cell cycle may be an all-or-none process in many instances. All-or-None Phosphorylation Phosphorylation is a key regulatory event that drives many cellular processes, including cell division. Olsen et al. undertook a phosphoproteomic analysis of HeLa cells at various stages in the cell cycle, which linked new phosphorylation sites and kinase substrates to specific stages. Furthermore, they established a method to calculate the fractional occupancy of… Expand

Paper Mentions

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The emerging roles of PPPs in mitosis and their regulation of and by mitotic kinases are discussed, as well as mechanisms that determine PPP substrate recognition and specificity are discussed. Expand
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References

SHOWING 1-10 OF 67 REFERENCES
A quantitative atlas of mitotic phosphorylation
TLDR
Analysis of non-proline site-containing phosphopeptides identified two unique motifs that suggest there are at least two undiscovered mitotic kinases, suggesting that many of the proteins identified may be CDK substrates. Expand
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
TLDR
This work combines kinase-selective affinity purification with quantitative mass spectrometry to analyze the cell-cycle regulation of protein kinases and reveals numerous unknown M phase-induced phosphorylation sites on kinases with established mitotic functions. Expand
Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
TLDR
A general mass spectrometric technology is developed and applied for identification and quantitation of phosphorylation sites as a function of stimulus, time, and subcellular location to provide a missing link in a global, integrative view of cellular regulation. Expand
Global and site-specific quantitative phosphoproteomics: principles and applications.
TLDR
Enrichment strategies and methods for mass spectrometric fragmentation and analysis of phosphopeptides are reviewed and different quantitative methods and their application to problems in cell signaling and drug target discovery are described. Expand
Linear Motif Atlas for Phosphorylation-Dependent Signaling
TLDR
The resulting atlas of linear motifs revealed that oncogenic kinases tends to be less specific in the target sequences they phosphorylate than their non-oncogenic counterparts, that autophosphorylation sites tend to be more variable than other substrates of a given kinase, and that coupling interaction domains with kinase domains may allow phosphorylation site specificity to be low while still maintaining substrate specificity. Expand
Different phosphorylation states of the anaphase promoting complex in response to antimitotic drugs: A quantitative proteomic analysis
TLDR
It is shown that during drug arrest the phosphorylation state of the APC changes, indicating that the mitotic arrest is not a static condition, and this findings are discussed in terms of the variable efficacy of antimitotic drugs in cancer chemotherapy. Expand
Phospho.ELM: A database of experimentally verified phosphorylation sites in eukaryotic proteins
TLDR
This work states that Phospho.ELM will be a valuable tool both for molecular biologists working on protein phosphorylation sites and for bioinformaticians developing computational predictions on the specificity of phosphorylated reactions. Expand
PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation
TLDR
As it develops into a comprehensive resource of known in vivo phosphorylation sites, it is expected that PhosphoSite will be a valuable tool for researchers seeking to understand the role of intracellular signaling pathways in a wide variety of biological processes. Expand
NetworKIN: a resource for exploring cellular phosphorylation networks
TLDR
How NetworKIN can be used for both global and targeted molecular studies is described, including how the resource offers insight into phosphorylation-modulated interaction networks. Expand
Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis
TLDR
Results indicated a novel mechanism that Cdk1 regulated mitotic vimentin phosphorylation via not only a direct enzyme reaction but also Plk1 recruitment to vimentsin. Expand
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