| Autor: |
Akihiro Harada, Masataka Kunii, Kazuo Kurokawa, Takuya Sumi, Satoshi Kanda, Yu Zhang, Satomi Nadanaka, Koichiro M. Hirosawa, Kazuaki Tokunaga, Takuro Tojima, Manabu Taniguchi, Kenta Moriwaki, Shin-ichiro Yoshimura, Miki Yamamoto-Hino, Satoshi Goto, Toyomasa Katagiri, Satoshi Kume, Mitsuko Hayashi-Nishino, Miyako Nakano, Eiji Miyoshi, Kenichi G. N. Suzuki, Hiroshi Kitagawa, Akihiko Nakano |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
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| Zdroj: |
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2041-1723 |
| DOI: |
10.1038/s41467-024-48901-1 |
| Popis: |
Abstract Knowledge on the distribution and dynamics of glycosylation enzymes in the Golgi is essential for better understanding this modification. Here, using a combination of CRISPR/Cas9 knockin technology and super-resolution microscopy, we show that the Golgi complex is assembled by a number of small ‘Golgi units’ that have 1-3 μm in diameter. Each Golgi unit contains small domains of glycosylation enzymes which we call ‘zones’. The zones of N- and O-glycosylation enzymes are colocalised. However, they are less colocalised with the zones of a glycosaminoglycan synthesizing enzyme. Golgi units change shapes dynamically and the zones of glycosylation enzymes rapidly move near the rim of the unit. Photobleaching analysis indicates that a glycosaminoglycan synthesizing enzyme moves between units. Depletion of giantin dissociates units and prevents the movement of glycosaminoglycan synthesizing enzymes, which leads to insufficient glycosaminoglycan synthesis. Thus, we show the structure-function relationship of the Golgi and its implications in human pathogenesis. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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