title: Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation.
abstract: The nutrient sensor, O-linked N-acetylglucosamine (O-GlcNAc), cycles on and off nuclear and cytosolic proteins to regulate many cellular processes, including transcription and signaling. Dysregulated O-GlcNAcylation and its interplay with phosphorylation contribute to the etiology of diabetes, cancer, and neurodegeneration. Herein, we review recent findings about O-GlcNAc's regulation of cell physiology.
authors.affiliation: Department of Biological Chemistry, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA. Electronic address: shardiv1@jhmi.edu.
authors.forename: Stéphan
authors.initials: S
authors.lastname: Hardivillé
authors.affiliation: Department of Biological Chemistry, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA. Electronic address: gwhart@jhmi.edu.
authors.forename: Gerald W
authors.initials: GW
authors.lastname: Hart
mesh_terms: D055372:AMP-Activated Protein Kinases / Q000378:metabolism; D000117:Acetylglucosamine / Q000378:metabolism*; D003920:Diabetes Mellitus / Q000378:metabolism / Q000473:pathology; D057890:Epigenomics; D006031:Glycosylation; D006801:Humans; D009369:Neoplasms / Q000378:metabolism / Q000473:pathology; D015398:Signal Transduction; D014158:Transcription, Genetic
chemical_list: D055372:AMP-Activated Protein Kinases; D000117:Acetylglucosamine
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