Modulation of synaptic transmission through O-GlcNAcylation

Seunghyo Han; Jun Nyeong Kim; Chan Ho Park; Jin Seok Byun; Do Yeon Kim; Hyoung Gon Ko

doi:10.1186/s13041-023-01072-4

Modulation of synaptic transmission through O-GlcNAcylation

Seunghyo Han, Jun Nyeong Kim, Chan Ho Park, Jin Seok Byun, Do Yeon Kim, Hyoung Gon Ko

Department of Dentistry

Kyungpook National University

Research output: Contribution to journal › Review article › peer-review

1 Scopus citations

Abstract

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.

Original language	English
Article number	1
Journal	Molecular Brain
Volume	17
Issue number	1
DOIs	https://doi.org/10.1186/s13041-023-01072-4
State	Published - Dec 2024

Keywords

O-GlcNAc transferase
O-GlcNAcase
O-GlcNAcylation
Synaptic plasticity
Synaptic transmission

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1186/s13041-023-01072-4

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title = "Modulation of synaptic transmission through O-GlcNAcylation",

abstract = "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.",

keywords = "O-GlcNAc transferase, O-GlcNAcase, O-GlcNAcylation, Synaptic plasticity, Synaptic transmission",

author = "Seunghyo Han and Kim, {Jun Nyeong} and Park, {Chan Ho} and Byun, {Jin Seok} and Kim, {Do Yeon} and Ko, {Hyoung Gon}",

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year = "2024",

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doi = "10.1186/s13041-023-01072-4",

language = "English",

volume = "17",

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T1 - Modulation of synaptic transmission through O-GlcNAcylation

AU - Han, Seunghyo

AU - Kim, Jun Nyeong

AU - Park, Chan Ho

AU - Byun, Jin Seok

AU - Kim, Do Yeon

AU - Ko, Hyoung Gon

PY - 2024/12

Y1 - 2024/12

N2 - 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.

AB - 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.

KW - O-GlcNAc transferase

KW - O-GlcNAcase

KW - O-GlcNAcylation

KW - Synaptic plasticity

KW - Synaptic transmission

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U2 - 10.1186/s13041-023-01072-4

DO - 10.1186/s13041-023-01072-4

M3 - Review article

C2 - 38167470

AN - SCOPUS:85181234903

SN - 1756-6606

VL - 17

JO - Molecular Brain

JF - Molecular Brain

IS - 1

M1 - 1

ER -

Modulation of synaptic transmission through O-GlcNAcylation

Abstract

Keywords

UN SDGs

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