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

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-transfera...

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Autores principales: Yoon, Danbi, Moon, Ju Heun, Cho, Anna, Boo, Hyejoon, Cha, Jeong Seok, Lee, Yoonji, Yoo, Jiho
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Molecular and Cellular Biology 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10258461/
https://www.ncbi.nlm.nih.gov/pubmed/37190766
http://dx.doi.org/10.14348/molcells.2023.0001
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author Yoon, Danbi
Moon, Ju Heun
Cho, Anna
Boo, Hyejoon
Cha, Jeong Seok
Lee, Yoonji
Yoo, Jiho
author_facet Yoon, Danbi
Moon, Ju Heun
Cho, Anna
Boo, Hyejoon
Cha, Jeong Seok
Lee, Yoonji
Yoo, Jiho
author_sort Yoon, Danbi
collection PubMed
description 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.
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spelling pubmed-102584612023-06-13 Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin Yoon, Danbi Moon, Ju Heun Cho, Anna Boo, Hyejoon Cha, Jeong Seok Lee, Yoonji Yoo, Jiho Mol Cells Minireview 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. Korean Society for Molecular and Cellular Biology 2023-06-30 2023-05-16 /pmc/articles/PMC10258461/ /pubmed/37190766 http://dx.doi.org/10.14348/molcells.2023.0001 Text en © The Korean Society for Molecular and Cellular Biology. All rights reserved. https://creativecommons.org/licenses/by-nc-sa/3.0/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/ (https://creativecommons.org/licenses/by-nc-sa/3.0/)
spellingShingle Minireview
Yoon, Danbi
Moon, Ju Heun
Cho, Anna
Boo, Hyejoon
Cha, Jeong Seok
Lee, Yoonji
Yoo, Jiho
Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin
title Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin
title_full Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin
title_fullStr Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin
title_full_unstemmed Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin
title_short Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin
title_sort structure-based insight on the mechanism of n-glycosylation inhibition by tunicamycin
topic Minireview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10258461/
https://www.ncbi.nlm.nih.gov/pubmed/37190766
http://dx.doi.org/10.14348/molcells.2023.0001
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