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O-Linked β-N-acetylglucosamine
''O''-Linked β-''N''-acetylglucosamine (O-GlcNAc) is an intracellular carbohydrate that dynamically modifies the amino acids serine and threonine through their hydroxyl moieties on nuclear and cytoplasmic proteins. As a form of protein glycosylation, it differs from most other forms in three aspects: first, it occurs exclusively within the nuclear and cytoplasmic compartments of the cell; secondly, it is generally not elongated or modified to form more complex structures; lastly it is attached and removed multiple times in the life of a polypeptide, often cycling at rapid, different rates on different sites.
== Background ==
O-linked GlcNAc was first discovered in 1983; when probing for GlcNAc-terminating glycoconjugates in thymocytes, lymphocytes and macrophages, analyses showed most galactosylated (glycosylation using galactose) glycans existed within the cell as single O-linked GlcNAc varieties.
Protein glycosylation has long been regarded not to occur in the cytoplasmic/nuclear compartments of the cell.〔Comer, F.I. and Hart, G.W. (2000) O-glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate. J. Biol. Chem.,275, 29179–29182.〕 However, research during the past two decades has clearly shown that O-GlcNAc is one of the most abundant posttranslational modifications within the nucleocytoplasmic compartments of all members of the Metazoan division, including animals, the viruses that infect them, and plants. It is found on hundreds, if not thousands, of nucleocytoplasmic proteins, and in fact many of the most heavily studied proteins in biology are O-GlcNAcylated. There has been no evidence of O-GlcNAc outside of cells.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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