Quantitative site-specific phosphorylation dynamics of human protein kinases during mitotic progression

Dulla, K. and Daub, H. and Hornberger, R. and Nigg, E. A. and Korner, R.. (2010) Quantitative site-specific phosphorylation dynamics of human protein kinases during mitotic progression. Molecular & cellular proteomics, Vol. 9, H. 6. pp. 1167-1181.

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Official URL: http://edoc.unibas.ch/dok/A5842437

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Reversible protein phosphorylation is a key regulatory mechanism of mitotic progression. Importantly, protein kinases themselves are also regulated by phosphorylation-dephosphorylation processes, hence phosphorylation dynamics of kinases hold a wealth of information about phosphorylation networks. Here, we investigated the site-specific phosphorylation dynamics of human kinases during mitosis using synchronization of HeLa S cells, kinase enrichment and high resolution mass spectrometry. In biological triplicate analyses, we identified 206 protein kinases (PKs) and more than 900 PK phosphorylation sites, including 61 phosphorylation sites on activation segments, and quantified their relative abundances across three specific mitotic stages. Around 25% of the kinase phosphorylation site ratios were found to be changed by at least 50% during mitotic progression. Further network analysis of jointly regulated kinase groups suggested that Cyclin-dependent kinase and mitogen-activated kinase centered interaction networks are coordinately down- and upregulated in late mitosis, respectively. Importantly, our data cover most of the already known mitotic kinases and, moreover, identify attractive candidates for future studies of phosphorylation-based mitotic signaling. Thus, the results of this study provide a valuable resource for cell biologists and provide insight into the systems properties of the mitotic phosphokinome.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Cell Biology (Nigg)
UniBasel Contributors:Nigg, Erich A.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:The American Society for Biochemistry and Molecular Biology
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Jun 2012 06:56
Deposited On:08 Jun 2012 06:51

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