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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Bibliographic Details
Published inMolecules and cells Vol. 46; no. 6; pp. 337 - 344
Main Authors Danbi Yoon, Ju Heun Moon, Anna Cho, Hyejoon Boo, Jeong Seok Cha, Yoonji Lee, Jiho Yoo
Format Journal Article
LanguageKorean
Published 2023
Subjects
DPAGT1
GlcNAc-1-P transferase
GPT
N-glycosylation
tunicamycin
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Summary: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.
Bibliography:KISTI1.1003/JNL.JAKO202320664646731
ISSN:1016-8478
0219-1032