{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Gyenis L"],"funding":["Natural Sciences and Engineering Research Council of Canada","Canadian Institutes of Health Research"],"pubmed_abstract":["Casein Kinase 2 (CSNK2) is an extremely pleiotropic, ubiquitously expressed protein kinase involved in the regulation of numerous key biological processes. Mapping the CSNK2-dependent phosphoproteome is necessary for better characterization of its fundamental role in cellular signalling. While ATP-competitive inhibitors have enabled the identification of many putative kinase substrates, compounds targeting the highly conserved ATP-binding pocket often exhibit off-target effects limiting their utility for definitive kinase-substrate assignment. To overcome this limitation, we devised a strategy combining chemical genetics and quantitative phosphoproteomics to identify and validate CSNK2 substrates. We engineered U2OS cells expressing exogenous wild type CSNK2A1 (WT) or a triple mutant (TM, "],"journal":["Frontiers in molecular biosciences"],"pagination":["909711"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9225150"],"repository":["biostudies-literature"],"pubmed_title":["Chemical Genetic Validation of CSNK2 Substrates Using an Inhibitor-Resistant Mutant in Combination with Triple SILAC Quantitative Phosphoproteomics."],"pmcid":["PMC9225150"],"pubmed_authors":["Litchfield DW","Pittock P","Nunez de Villavicencio Diaz T","Turowec JP","Menyhart D","Cruise ES","Gyenis L","Chai DB","Desormeaux PJ","Fess SR","Lajoie G","Trifoi F","Jurcic K","Rabalski AJ","Zukowski SA","Roffey SE"],"additional_accession":[]},"is_claimable":false,"name":"Chemical Genetic Validation of CSNK2 Substrates Using an Inhibitor-Resistant Mutant in Combination with Triple SILAC Quantitative Phosphoproteomics.","description":"Casein Kinase 2 (CSNK2) is an extremely pleiotropic, ubiquitously expressed protein kinase involved in the regulation of numerous key biological processes. Mapping the CSNK2-dependent phosphoproteome is necessary for better characterization of its fundamental role in cellular signalling. While ATP-competitive inhibitors have enabled the identification of many putative kinase substrates, compounds targeting the highly conserved ATP-binding pocket often exhibit off-target effects limiting their utility for definitive kinase-substrate assignment. To overcome this limitation, we devised a strategy combining chemical genetics and quantitative phosphoproteomics to identify and validate CSNK2 substrates. We engineered U2OS cells expressing exogenous wild type CSNK2A1 (WT) or a triple mutant (TM, ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-04-08T09:45:45.096Z","creation":"2024-11-19T16:31:22.391Z"},"accession":"S-EPMC9225150","cross_references":{"pubmed":["35755813"],"doi":["10.3389/fmolb.2022.909711"]}}