Modulation of synaptic transmission through O-GlcNAcylation

• Published in: Molecular brain Vol. 17; no. 1; p. 1
• Main Authors: Han, Seunghyo, Kim, Jun-Nyeong, Park, Chan Ho, Byun, Jin-Seok, Kim, Do-Yeon, Ko, Hyoung-Gon
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 02.01.2024; BioMed Central; BMC
• Subjects: Amino acids; Cyclic AMP response element-binding protein; Diabetes Mellitus; Enzymes; Genetic aspects; Humans; Kinases; N-Acetylglucosamine; Nano Review; Nervous system; Neuromodulation; Neurons; Neurons - physiology; Neurophysiology; Neurosciences; O-GlcNAc transferase; O-GlcNAcase; O-GlcNAcylation; Phosphorylation; Post-translational modification; Protein Processing, Post-Translational; Proteins; Synapsin; Synaptic plasticity; Synaptic Transmission; Threonine; α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors; New York; United States > US; O-GlcNAcase; O-GlcNAcylation; O-GlcNAc transferase; Synaptic transmission; Synaptic plasticity
• ISSN: 1756-6606; 1756-6606
• 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.