| Autor: |
Yagi H; Graduate School of Pharmaceutical Sciences, Nagoya City University.; Exploratory Research Center on Life and Living Systems (ExCELLS)., Tateo S; Exploratory Research Center on Life and Living Systems (ExCELLS).; Institute for Molecular Science, National Institutes of Natural Sciences., Saito T; Exploratory Research Center on Life and Living Systems (ExCELLS).; Institute for Molecular Science, National Institutes of Natural Sciences., Ohta Y; Exploratory Research Center on Life and Living Systems (ExCELLS)., Nishi E; Exploratory Research Center on Life and Living Systems (ExCELLS)., Obitsu S; Exploratory Research Center on Life and Living Systems (ExCELLS)., Suzuki T; Exploratory Research Center on Life and Living Systems (ExCELLS).; Institute for Molecular Science, National Institutes of Natural Sciences., Seetaha S; Exploratory Research Center on Life and Living Systems (ExCELLS).; Institute for Molecular Science, National Institutes of Natural Sciences.; Department of Biochemistry, Faculty of Science, Kasetsart University., Hellec C; Graduate School of Pharmaceutical Sciences, Nagoya City University., Nakano A; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics., Tojima T; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics., Kato K; Graduate School of Pharmaceutical Sciences, Nagoya City University.; Exploratory Research Center on Life and Living Systems (ExCELLS).; Institute for Molecular Science, National Institutes of Natural Sciences. |
| Jazyk: |
angličtina |
| Zdroj: |
Cell structure and function [Cell Struct Funct] 2024 Aug 27; Vol. 49 (2), pp. 47-55. Date of Electronic Publication: 2024 Aug 22. |
| DOI: |
10.1247/csf.24008 |
| Abstrakt: |
The Golgi apparatus, a crucial organelle involved in protein processing, including glycosylation, exhibits complex sub-structures, i.e., cis-, medial, and trans-cisternae. This study investigated the distribution of glycosyltransferases within the Golgi apparatus of mammalian cells via 3D super-resolution imaging. Focusing on human glycosyltransferases involved in N-glycan modification, we found that even enzymes presumed to coexist in the same Golgi compartment exhibit nuanced variations in localization. By artificially making their N-terminal regions [composed of a cytoplasmic, transmembrane, and stem segment (CTS)] identical, it was possible to enhance the degree of their colocalization, suggesting the decisive role of this region in determining the sub-Golgi localization of enzymes. Ultimately, this study reveals the molecular codes within CTS regions as key determinants of glycosyltransferase localization, providing insights into precise control over the positioning of glycosyltransferases, and consequently, the interactions between glycosyltransferases and substrate glycoproteins as cargoes in the secretory pathway. This study advances our understanding of Golgi organization and opens avenues for programming the glycosylation of proteins for clinical applications.Key words: Golgi apparatus, glycosyltransferase, 3D super-resolution imaging, N-glycosylation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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