1. Dynamic movement of the Golgi unit and its glycosylation enzyme zones
- Author
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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, and Akihiko Nakano
- Subjects
Science - Abstract
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.
- Published
- 2024
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