Global identification of O-GlcNAc-modified proteins

Animesh Nandi, Robert Sprung, Deb K. Barma, Yingxin Zhao, Sung Chan Kim, John R. Falck, Yingming Zhao

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Abstract

The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational 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.

Original languageEnglish (US)
Pages (from-to)452-458
Number of pages7
JournalAnalytical Chemistry
Volume78
Issue number2
DOIs
StatePublished - Jan 15 2006

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ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

Nandi, A., Sprung, R., Barma, D. K., Zhao, Y., Kim, S. C., Falck, J. R., & Zhao, Y. (2006). Global identification of O-GlcNAc-modified proteins. Analytical Chemistry, 78(2), 452-458. https://doi.org/10.1021/ac051207j