GLCNAC-PROBE · Novel chemical and enzymatic strategies for probing O-GlcNAc glycosylation

The modification of nuclear and cytoplasmic proteins by covalent attachment of N-acetylglucosamine (O-GlcNAc) to serine or threonine residues is emerging as a crucial regulatory posttranslational modification similar to phosphorylation. O-GlcNAc is essential for cell survival and is implicated in key biological processes (e. g., nutrient sensing, protein regulation and gene expression) and human diseases (e. g., diabetes, Alzheimer’s disease and cancer). In contrast to conventional protein glycosylation, O-GlcNAcylation is not further elaborated into complex glycans and occurs on intracellular proteins.Despite its biological importance, the functional roles and molecular details of O-GlcNAc modification remain to be elucidated