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Mol. Cells 2023; 46(6): 337-344

Published online May 16, 2023

https://doi.org/10.14348/molcells.2023.0001

© The Korean Society for Molecular and Cellular Biology

Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin

Danbi Yoon , Ju Heun Moon , Anna Cho , Hyejoon Boo , Jeong Seok Cha *, Yoonji Lee *, and Jiho Yoo *

College of Pharmacy, Chung-Ang University, Seoul 06974, Korea

Correspondence to : pickcha1121@cau.ac.kr(JSC), yoonjilee@cau.ac.kr(YL), jyoo@cau.ac.kr(JY)

Received: January 1, 2023; Revised: February 14, 2023; Accepted: February 20, 2023

This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/.

Abstract

N-glycosylation, a common post-translational modification, is widely acknowledged to have a significant effect on protein stability and folding. N-glycosylation is a complex process that occurs in the endoplasmic reticulum (ER) and requires the participation of multiple enzymes. GlcNAc-1-P-transferase (GPT) is essential for initiating N-glycosylation in the ER. Tunicamycin is a natural product that inhibits N-glycosylation and produces ER stress, and thus it is utilized in research. The molecular mechanism by which GPT triggers N-glycosylation is discussed in this review based on the GPT structure. Based on the structure of the GPT-tunicamycin complex, we also discuss how tunicamycin reduces GPT activity, which prevents N-glycosylation. This review will be highly useful for understanding the role of GPT in the N-glycosylation of proteins, as well as presents a potential for considering tunicamycin as an antibiotic treatment.

Keywords DPAGT1, GlcNAc-1-P transferase, GPT, N-glyco­sylation, tunicamycin

Article

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Mol. Cells 2023; 46(6): 337-344

Published online June 30, 2023 https://doi.org/10.14348/molcells.2023.0001

Copyright © The Korean Society for Molecular and Cellular Biology.

Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin

Danbi Yoon , Ju Heun Moon , Anna Cho , Hyejoon Boo , Jeong Seok Cha *, Yoonji Lee *, and Jiho Yoo *

College of Pharmacy, Chung-Ang University, Seoul 06974, Korea

Correspondence to:pickcha1121@cau.ac.kr(JSC), yoonjilee@cau.ac.kr(YL), jyoo@cau.ac.kr(JY)

Received: January 1, 2023; Revised: February 14, 2023; Accepted: February 20, 2023

This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/.

Abstract

N-glycosylation, a common post-translational modification, is widely acknowledged to have a significant effect on protein stability and folding. N-glycosylation is a complex process that occurs in the endoplasmic reticulum (ER) and requires the participation of multiple enzymes. GlcNAc-1-P-transferase (GPT) is essential for initiating N-glycosylation in the ER. Tunicamycin is a natural product that inhibits N-glycosylation and produces ER stress, and thus it is utilized in research. The molecular mechanism by which GPT triggers N-glycosylation is discussed in this review based on the GPT structure. Based on the structure of the GPT-tunicamycin complex, we also discuss how tunicamycin reduces GPT activity, which prevents N-glycosylation. This review will be highly useful for understanding the role of GPT in the N-glycosylation of proteins, as well as presents a potential for considering tunicamycin as an antibiotic treatment.

Keywords: DPAGT1, GlcNAc-1-P transferase, GPT, N-glyco­sylation, tunicamycin

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).

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