title: Use of a mutant OGA for detecting O-GlcNAc modified proteins.
abstract: In the previous issue of Biochemical Journal Mariappa et al. [(2015) Biochem J. 470,: 255-262] demonstrate a new method for visualizing O-linked N-acetylglucosamine (O-GlcNAc) modified proteins by making use of a catalytically dead version of the enzyme that normally removes this modification. They show their approach has broader specificity than current antibody-based techniques and higher specificity than lectin and chemical biology-based labelling approaches. This commentary discusses methods for O-GlcNAc detection and the significance of this work for characterizing this common, but currently poorly understood regulatory modification.
authors.affiliation: Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94143, U.S.A. chalkley@cgl.ucsf.edu.
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Chalkley
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D004330:Drosophila / Q000378:metabolism*; D006801:Humans; D001619:beta-N-Acetylhexosaminidases / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D001619:beta-N-Acetylhexosaminidases
keywords: O-linked N-acetylglucosamine (O-GlcNAc); OGA; glycosylation; mass spectrometry