title: Proteomic approaches for site-specific O-GlcNAcylation analysis.
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 its significance has been implicated in several disease states, such as metabolic diseases, cancer and neurological diseases. Yet it remains technically challenging to characterize comprehensively and quantitatively because of its low abundance, low stoichiometry and extremely labile nature under conventional collision-induced dissociation tandem MS conditions. Herein, we review the recent advances addressing these challenges in developing proteomic approaches for site-specific O-GlcNAcylation analysis, including specific enrichment of O-GlcNAc peptides/proteins, unambiguous site-determination of O-GlcNAc modification and quantitative analysis of O-GlcNAcylation.
authors.affiliation: Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, USA.
authors.forename: Sheng
authors.initials: S
authors.lastname: Wang
authors.forename: Feng
authors.initials: F
authors.lastname: Yang
authors.forename: David G
authors.initials: DG
authors.lastname: Camp
authors.forename: Karin
authors.initials: K
authors.lastname: Rodland
authors.forename: Wei-Jun
authors.initials: WJ
authors.lastname: Qian
authors.forename: Tao
authors.initials: T
authors.lastname: Liu
authors.forename: Richard D
authors.initials: RD
authors.lastname: Smith
mesh_terms: D000215:Acylation; D019943:Amino Acid Substitution; D005998:Glycine / Q000737:chemistry*; D006801:Humans; D040901:Proteomics / Q000379:methods*; D013329:Structure-Activity Relationship
chemical_list: D005998:Glycine