Department of Anatomy and Neurobiology, School of Dentistry, Brain Science and Engineering Institute, Kyungpook National University, 2177 Dalgubeol-daero, Daegu, 41940, South Korea.
Department of Dental Biomaterials, School of Dentistry, Kyungpook National University, Daegu, 41940, Republic of Korea.
Mol Brain. 2024 Jan 2;17(1):1. doi: 10.1186/s13041-023-01072-4.
O-GlcNAcylation is a posttranslational modification where N-acetylglucosamine (O-GlcNAc) is attached and detached from a serine/threonine position by two enzymes: O-GlcNAc transferase and O-GlcNAcase. In addition to roles in diabetes and cancer, recent pharmacological and genetic studies have revealed that O-GlcNAcylation is involved in neuronal function, specifically synaptic transmission. Global alteration of the O-GlcNAc level does not affect basal synaptic transmission while the effect on synaptic plasticity is unclear. Although synaptic proteins that are O-GlcNAcylated are gradually being discovered, the mechanism of how O-GlcNAcylated synaptic protein modulate synaptic transmission has only been reported on CREB, synapsin, and GluA2 subunit of AMPAR. Future research enabling the manipulation of O-GlcNAcylation in individual synaptic proteins should reveal hidden aspects of O-GlcNAcylated synaptic proteins as modulators of synaptic transmission.
O-糖基化是一种翻译后修饰，通过两种酶：O-连接的 N-乙酰葡萄糖胺转移酶（O-GlcNAc transferase）和 O-连接的 N-乙酰葡萄糖胺酶（O-GlcNAcase），将 N-乙酰葡萄糖胺（O-GlcNAc）连接和分离到丝氨酸/苏氨酸位置上。除了在糖尿病和癌症中的作用外，最近的药理学和遗传学研究表明，O-糖基化参与神经元功能，特别是突触传递。O-GlcNAc 水平的全局改变不会影响基础突触传递，而对突触可塑性的影响尚不清楚。尽管逐渐发现了 O-糖基化的突触蛋白，但 O-GlcNAc 化的突触蛋白如何调节突触传递的机制仅在 CREB、突触素和 AMPAR 的 GluA2 亚基上有报道。未来的研究能够在单个突触蛋白中操纵 O-GlcNAc 化，应该揭示 O-GlcNAc 化的突触蛋白作为突触传递调节剂的隐藏方面。
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