O-linked β-N-acetylglucosamine modification and its biological functions

The covalent attachment of O-linked β-N- acetylglucosamine （O-GIcNAc） to Ser/Thr residues of proteins acts as not only a posttranslational modification but also a nutritional sensor in nucleus and cytoplasm, which directly regulates the expression of genes and multiple crucial signal transduction pathways. Dynamic O- GlcNAcylation at Ser/Thr residues is catalyzed by two key enzymes, O-GIcNAc transferase （OGT） and O-GlcNAcase, which are responsible for addition and removal of the O- GlcNAc modification, respectively. O-GlcNAc modifica- tion plays important roles in cellular signaling in animals, especially in human diseases. Two orthologs of OGT in plants, SECRET AGENT and SPINDLY, have been reported to be involved in diverse plant processes. However, compared with the functional mechanisms revealed in animals, the consequences of protein O-GlcNAc modifi- cation in plants is largely unknown, and the relationship between O-GlcNAcylation and cellular processes needs to be explored. In this review, we summarized the recent advances on O-GlcNAc modification and its biological functions in animals and plants, and prospect of more special functions of O-GlcNAc will be revealed in plants.

到蛋白质的 Ser/Thr 残余的连接 O 的 -N-acetylglucosamine (O-GlcNAc ) 的共有原子价附件在原子核和细胞质充当不仅 posttranslational 修正而且一个营养的传感器，它直接调整基因和多重关键信号 transduction 小径的表示。在 Ser/Thr 残余的动态 O-GlcNAcylation 被二关键酶， O-GlcNAc transferase (OGT ) 和 O-GlcNAcase 催化，它分别地为 O-GlcNAc 修正的增加和移动负责。O-GlcNAc 修正在在动物的细胞的发信号起重要作用，特别在人的疾病。在植物的 OGT 的二 orthologs，敌探并且细长纤弱，被报导了涉及多样的植物过程。然而与在动物揭示的功能的机制相比，蛋白质 O-GlcNAc 的后果在植物的修正大部分是未知的，并且在 O-GlcNAcylation 之间的关系和细胞的过程需要被探索。在这评论，我们在动物在 O-GlcNAc 修正和它的生物功能上总结了最近的进展， O-GlcNAc 的更特殊的功能的植物，和前景将在植物被揭示。