Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin.
Mol Cells
; 46(6): 337-344, 2023 Jun 30.
Article
in En
| MEDLINE
| ID: mdl-37190766
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Processing, Post-Translational
/
Endoplasmic Reticulum Stress
Language:
En
Journal:
Mol Cells
Journal subject:
BIOLOGIA MOLECULAR
Year:
2023
Document type:
Article