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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Korean Society for Molecular and Cellular Biology
2023
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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. |
format | Online Article Text |
id | pubmed-10258461 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Korean Society for Molecular and Cellular Biology |
record_format | MEDLINE/PubMed |
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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