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Proteome Wide Purification and Identification of O-GlcNAc-Modified Proteins Using Click Chemistry and Mass Spectrometry

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† Chair for Proteomics and Bioanalytics, Center of Life and Food Sciences, Weihenstephan, Technische Universität München, Freising, Germany
‡ Life Technologies, Eugene, Oregon 97402, United States
§ The MRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dundee, Scotland
∥ Center for Integrated Protein Science, Munich, Germany
*E-mail: [email protected]. Tel: +49 8161 715696. Fax: +49 8161 715931.
Cite this: J. Proteome Res. 2013, 12, 2, 927–936
Publication Date (Web):January 9, 2013
https://doi.org/10.1021/pr300967y
Copyright © 2013 American Chemical Society
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    Abstract

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    The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases. Despite its emerging biological significance, the systematic identification of O-GlcNAc proteins is still challenging. In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin. On-resin proteolysis using trypsin followed by LC–MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line. Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins. To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins. About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.

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