期刊
ACS CHEMICAL BIOLOGY
卷 14, 期 1, 页码 4-10出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.8b01052
关键词
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资金
- National Science Foundation of China (NSFC) [91753125, 31322019, 31570804, 81673387]
- National Key Research and Development Program of China [2016YFA0100303]
- Beijing Nova Program [Z161100004916163]
- National Science Foundation of Zhejiang Province [LR15C050001]
O-linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous post-translational modification of proteins and is essential for cell function. Quantifying the dynamics of O-GlcNAcylation in a proteome-wide level is critical for uncovering cellular mechanisms and functional roles of O-GlcNAcylation in cells. Here, we develop an isotope-coded photocleavable probe for profiling protein O-GlcNAcylation dynamics using quantitative mass spectrometry-based proteomics. This probe enables selective tagging and isotopic labeling of O-GlcNAcylated proteins in one step from complex cellular mixtures. We demonstrate the application of the probe to quantitatively profile O-GlcNAcylation sites in 293T cells upon chemical induction of O-GlcNAc levels. We further applied the probe to quantitatively analyze the stoichiometry of O-GlcNAcylation between sorafenib-sensitive and sorafenib-resistant liver cancer cells, which lays the foundation for mechanistic investigation of O-GlcNAcylation in regulating cancer chemoresistance. Thus, this probe provides a powerful tool to profile O-GlcNAcylation dynamics in cells.
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