title: O-GlcNAc cycling: how a single sugar post-translational modification is changing the way we think about signaling networks.
abstract: O-GlcNAc is an ubiquitous post-translational protein modification consisting of a single N-acetlyglucosamine moiety linked to serine or threonine residues on nuclear and cytoplasmic proteins. Recent work has begun to uncover the functional roles of O-GlcNAc in cellular processes. O-GlcNAc modified proteins are involved in sensing the nutrient status of the surrounding cellular environment and adjusting the activity of cellular proteins accordingly. O-GlcNAc regulates cellular responses to hormones such as insulin, initiates a protective response to stress, modulates a cell's capacity to grow and divide, and regulates gene transcription. This review will focus on recent work involving O-GlcNAc in sensing the environment and regulating signaling cascades.
authors.affiliation: Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: Chad
authors.initials: C
authors.lastname: Slawson
authors.forename: Michael P
authors.initials: MP
authors.lastname: Housley
authors.forename: Gerald W
authors.initials: GW
authors.lastname: Hart
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D006801:Humans; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction; D014158:Transcription, Genetic
chemical_list: D000117:Acetylglucosamine