期刊
ANALYTICAL CHEMISTRY
卷 78, 期 2, 页码 452-458出版社
AMER CHEMICAL SOC
DOI: 10.1021/ac051207j
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资金
- NCI NIH HHS [CA 107943] Funding Source: Medline
The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant post-translational modification present in cytosolic and nuclear proteins. The functions and subproteome of O-GlcNAc modification remain largely undefined. Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins. The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies. Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation. Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
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