Abstract
Mass spectrometry-based in vitro kinase screens play an essential role in the discovery of kinase substrates, however, many suffer from biological and technical noise or necessitate genetically-altered enzyme-cofactor systems. We describe a method that combines stable γ-[(18)O2]-ATP with classical in vitro kinase assays within a contemporary quantitative proteomic workflow. Our approach improved detection of known substrates of the non-receptor tyrosine kinase ABL1; and identified potential, new in vitro substrates.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / metabolism*
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Adenosine Triphosphate / analysis*
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Adenosine Triphosphate / chemistry*
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Amino Acid Sequence
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Chromatography, High Pressure Liquid
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Cytoskeletal Proteins / metabolism*
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DEAD-box RNA Helicases / chemistry
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HEK293 Cells
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Humans
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Kinetics
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Mass Spectrometry*
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Oxygen Isotopes / chemistry
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Peptides / chemistry
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Peptides / metabolism
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Phosphorylation
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Protein Kinases / metabolism
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Substrate Specificity
Substances
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ABI1 protein, human
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Adaptor Proteins, Signal Transducing
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Cytoskeletal Proteins
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Oxygen Isotopes
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Oxygen-18
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Peptides
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Adenosine Triphosphate
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Protein Kinases
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DDX3X protein, human
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DEAD-box RNA Helicases