title: O-GlcNAc signalling: implications for cancer cell biology.
abstract: O-GlcNAcylation is the covalent attachment of β-D-N-acetylglucosamine (GlcNAc) sugars to serine or threonine residues of nuclear and cytoplasmic proteins, and it is involved in extensive crosstalk with other post-translational modifications, such as phosphorylation. O-GlcNAcylation is becoming increasing realized as having important roles in cancer-relevant processes, such as cell signalling, transcription, cell division, metabolism and cytoskeletal regulation. However, currently little is known about the specific roles of aberrant O-GlcNAcylation in cancer. In this Opinion article, we summarize the current understanding of O-GlcNAcylation in cancer and its emerging functions in transcriptional regulation at the level of chromatin and transcription factors.
authors.affiliation: The Department of Biochemistry and Molecular Biology, Kansas University School of Medicine, 3,901 Rainbow Boulevard, Kansas City, Kansas 66160, USA.
authors.forename: Chad
authors.initials: C
authors.lastname: Slawson
authors.forename: Gerald W
authors.initials: GW
authors.lastname: Hart
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism*; D000215:Acylation; D002471:Cell Transformation, Neoplastic; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D058990:Molecular Targeted Therapy; D017351:N-Acetylglucosaminyltransferases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D009369:Neoplasms / Q000188:drug therapy / Q000201:enzymology* / Q000503:physiopathology; D015398:Signal Transduction; D013379:Substrate Specificity
chemical_list: D017351:N-Acetylglucosaminyltransferases; C449880:O-GlcNAc transferase; D000117:Acetylglucosamine