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• W2742828134 abstract "The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine/threonine residues of proteins is a ubiquitous posttranslational modification found in all multicellular organisms. Like phosphorylation, O-GlcNAc glycosylation (O-GlcNAcylation) is inducible and regulates a myriad of physiological and pathological processes. However, understanding the diverse functions of O-GlcNAcylation is often challenging due to the difficulty of detecting and quantifying the modification. Thus, robust methods to study O-GlcNAcylation are essential to elucidate its key roles in the regulation of individual proteins, complex cellular processes, and disease. In this chapter, we describe a set of chemoenzymatic labeling methods to (1) detect O-GlcNAcylation on proteins of interest, (2) monitor changes in both the total levels of O-GlcNAcylation and its stoichiometry on proteins of interest, and (3) enable mapping of O-GlcNAc to specific serine/threonine residues within proteins to facilitate functional studies. First, we outline a procedure for the expression and purification of a multiuse mutant galactosyltransferase enzyme (Y289L GalT). We then describe the use of Y289L GalT to modify O-GlcNAc residues with a functional handle, N-azidoacetylgalactosamine (GalNAz). Finally, we discuss several applications of the copper-catalyzed azide-alkyne cycloaddition click reaction to attach various alkyne-containing chemical probes to GalNAz and demonstrate how this functionalization of O-GlcNAc-modified proteins can be used to realize (1)-(3) above. Overall, these methods, which utilize commercially available reagents and standard protein analytical tools, will serve to advance our understanding of the diverse and important functions of O-GlcNAcylation." @default.
• W2742828134 created "2017-08-17" @default.
• W2742828134 creator A5012554206 @default.
• W2742828134 creator A5043365362 @default.
• W2742828134 creator A5043949890 @default.
• W2742828134 date "2018-01-01" @default.
• W2742828134 modified "2023-10-05" @default.
• W2742828134 title "Methods for the Detection, Study, and Dynamic Profiling of O-GlcNAc Glycosylation" @default.
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• W2742828134 doi "https://doi.org/10.1016/bs.mie.2017.06.009" @default.
• W2742828134 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5886303" @default.
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