Journal
CELL REPORTS
Volume 3, Issue 4, Pages 1306-1320Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2013.03.027
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Funding
- European Union 7th Framework project PROSPECTS (Proteomics Specification in Space and Time) [HEALTH-F4-2008-201648]
- SystemsX.ch project PhosphonetX and ERC advanced grant Proteomics v3.0 from the European Union [233226]
- European Union 7th Framework Marie Curie Actions IEF grant Cancer Kinome'' [236839]
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Cellular information processing via reversible protein phosphorylation requires tight control of the localization, activity, and substrate specificity of protein kinases, which to a large extent is accomplished by complex formation with other proteins. Despite their critical role in cellular regulation and pathogenesis, protein interaction information is available for only a subset of the 518 human protein kinases. Here we present a global proteomic analysis of complexes of the human CMGC kinase group. In addition to subgroup-specific functional enrichment and modularity, the identified 652 high-confidence kinase-protein interactions provide a specific biochemical context for many poorly studied CMGC kinases. Furthermore, the analysis revealed a kinase-kinase subnetwork and candidate substrates for CMGC kinases. Finally, the presented interaction proteome uncovered a large set of interactions with proteins genetically linked to a range of human diseases, including cancer, suggesting additional routes for analyzing the role of CMGC kinases in controlling human disease pathways.
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