PNNL

Abstract

O-GlcNAcylation is a dynamic protein post-translational modification of serine or threonine residues by an O-linked monosaccharide N-acetylglucosamine (O-GlcNAc). O-GlcNAcylation was discovered three decades ago, and it has been shown to contribute to various disease states, such as metabolic diseases, cancer and neurological diseases. Yet it remains technically difficult to characterize comprehensively and quantitatively, due to its exceptionally low abundance and extremely labile nature under conventional tandem mass spectrometry conditions. Herein, we review the recent efforts for tackling these challenges in developing proteomic approaches for site-specific O-GlcNAcylation analysis, such as specific enrichment of O-GlcNAc peptides/proteins, unambiguous site-determination of O-GlcNAc modification, and quantitative analysis of O-GlcNAcylation.