Yang Xiaoyong, Qian Kevin
Program in Integrative Cell Signaling and Neurobiology of Metabolism, Department of Comparative Medicine, Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
Nat Rev Mol Cell Biol. 2017 Jul;18(7):452-465. doi: 10.1038/nrm.2017.22. Epub 2017 May 10.
O-GlcNAcylation - the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to cytoplasmic, nuclear and mitochondrial proteins - is a post-translational modification that regulates fundamental cellular processes in metazoans. A single pair of enzymes - O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) - controls the dynamic cycling of this protein modification in a nutrient- and stress-responsive manner. Recent years have seen remarkable advances in our understanding of O-GlcNAcylation at levels that range from structural and molecular biology to cell signalling and gene regulation to physiology and disease. New mechanisms and functions of O-GlcNAcylation that are emerging from these recent developments enable us to begin constructing a unified conceptual framework through which the significance of this modification in cellular and organismal physiology can be understood.
O-连接的N-乙酰葡糖胺化作用(O-GlcNAcylation),即将O-连接的N-乙酰葡糖胺(O-GlcNAc)基团连接到细胞质、细胞核和线粒体蛋白上,是一种翻译后修饰,可调节后生动物的基本细胞过程。一对酶——O-GlcNAc转移酶(OGT)和O-GlcNAcase(OGA)——以营养和应激反应的方式控制这种蛋白质修饰的动态循环。近年来,我们对O-连接的N-乙酰葡糖胺化作用的理解取得了显著进展,其涉及从结构和分子生物学、细胞信号传导和基因调控到生理学和疾病等多个层面。这些最新进展中出现的O-连接的N-乙酰葡糖胺化作用的新机制和功能,使我们能够开始构建一个统一的概念框架,通过该框架可以理解这种修饰在细胞和机体生理学中的重要性。