The Protein Interaction Landscape of the Human CMGC Kinase Group
Copyright policy )The Protein Interaction Landscape of the Human CMGC Kinase Group
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.
Cell Reports, 3 (4)
ISSN:2666-3864
ISSN:2211-1247
- Department of Biology United States
- ETH Zurich Switzerland
- UNIVERSITAET ZUERICH Switzerland
- Department of Biology Switzerland
- Instituts Universitaires de Technologie France
Proteome, Transcription, Genetic, SX12 PhosphoNetX, QH301-705.5, INTERACTION NETWORK, STATISTICAL-MODEL, Protein Serine-Threonine Kinases, BETA-CATENIN, Cell Line, Substrate Specificity, PATHWAY, SX00 SystemsX.ch, 1300 General Biochemistry, Genetics and Molecular Biology, Tandem Mass Spectrometry, REVEALS, Humans, Protein Interaction Maps, Biology (General), PHOSPHORYLATION, 3-M SYNDROME, Biochemistry, cell and molecular biology, Chromatography, High Pressure Liquid, TFIIH, MUTATIONS, Glycogen Synthase Kinases, MASS-SPECTROMETRY, Protein-Tyrosine Kinases, Cyclin-Dependent Kinases, 570 Life sciences; biology, Mitogen-Activated Protein Kinases
Proteome, Transcription, Genetic, SX12 PhosphoNetX, QH301-705.5, INTERACTION NETWORK, STATISTICAL-MODEL, Protein Serine-Threonine Kinases, BETA-CATENIN, Cell Line, Substrate Specificity, PATHWAY, SX00 SystemsX.ch, 1300 General Biochemistry, Genetics and Molecular Biology, Tandem Mass Spectrometry, REVEALS, Humans, Protein Interaction Maps, Biology (General), PHOSPHORYLATION, 3-M SYNDROME, Biochemistry, cell and molecular biology, Chromatography, High Pressure Liquid, TFIIH, MUTATIONS, Glycogen Synthase Kinases, MASS-SPECTROMETRY, Protein-Tyrosine Kinases, Cyclin-Dependent Kinases, 570 Life sciences; biology, Mitogen-Activated Protein Kinases
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