Dynamic movement of the Golgi unit and its glycosylation enzyme zones

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
Additional contact information
Akihiro Harada: Osaka University
Masataka Kunii: Osaka University
Kazuo Kurokawa: RIKEN Center for Advanced Photonics
Takuya Sumi: Osaka University
Satoshi Kanda: Osaka University
Yu Zhang: Osaka University
Satomi Nadanaka: Kobe Pharmaceutical University
Koichiro M. Hirosawa: Gifu University, Gifu
Kazuaki Tokunaga: LTD.
Takuro Tojima: RIKEN Center for Advanced Photonics
Manabu Taniguchi: Osaka University
Kenta Moriwaki: Osaka University
Shin-ichiro Yoshimura: Osaka University
Miki Yamamoto-Hino: Rikkyo University, Toshima-ku
Satoshi Goto: Rikkyo University, Toshima-ku
Toyomasa Katagiri: National Institute of Biomedical Innovation, National Institutes of Biomedical Innovation, Health and Nutrition
Satoshi Kume: RIKEN Center for Biosystems Dynamics Research
Mitsuko Hayashi-Nishino: Osaka University
Miyako Nakano: Hiroshima University, Higashi-Hiroshima
Eiji Miyoshi: Osaka University Graduate School of Medicine
Kenichi G. N. Suzuki: Gifu University, Gifu
Hiroshi Kitagawa: Kobe Pharmaceutical University
Akihiko Nakano: RIKEN Center for Advanced Photonics

Nature Communications, 2024, vol. 15, issue 1, 1-19

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.

Date: 2024
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DOI: 10.1038/s41467-024-48901-1

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