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