MassIVE MSV000085575

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Quantitative SILAC phosphoproteomics and proteomics of HL60 cells treated with covalent CDK7 inhibitor SY351

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Description

Using the covalent inhibitor SY-351 and quantitative SILAC phosphoproteomics, we identified CDK7 kinase substrates in human cells. We performed a double-label SILAC phosphoproteomics experiment, in which we metabolically labeled HL60 cells with light labeled (Lys0, Arg0) or heavy labeled (Lys8, Arg8) amino acids, which were treated with vehicle (DMSO) or 50 nM SY-351, followed by phosphopeptide enrichment and mass spectrometry analysis. The experimental design included two biological replicates of SY-351 treated heavy cells compared with DMSO treated light cells, a label-flip biological replicate of SY-351 light cells compared with DMSO treated heavy cells, and a null condition for which both heavy and light were treated with DMSO. The label-flip and null conditions control for systematic errors in phosphopeptide Heavy:Light SILAC ratios that are independent of the SY-351 treatment effect. We used a linear statistical model to capture these systematic errors, which improved our statistical power to detect phosphorylation sites that changed in abundance with SY-351 treatment. [doi:10.25345/C5PH8X] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: CDK7 phosphoproteomics SY351

Contact

Principal Investigators:
(in alphabetical order) 		Dylan J Taatjes, University of Colorado Boulder, United States
William Old, University of Colorado Boulder, United States
Submitting User: wold_cub
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