Dynamic movement of the Golgi unit and its glycosylation enzyme zones

• Published in: Nature communications Vol. 15; no. 1; p. 4514
• Main Authors: Harada, Akihiro, Kunii, Masataka, Kurokawa, Kazuo, Sumi, Takuya, Kanda, Satoshi, Zhang, Yu, Nadanaka, Satomi, Hirosawa, Koichiro M., Tokunaga, Kazuaki, Tojima, Takuro, Taniguchi, Manabu, Moriwaki, Kenta, Yoshimura, Shin-ichiro, Yamamoto-Hino, Miki, Goto, Satoshi, Katagiri, Toyomasa, Kume, Satoshi, Hayashi-Nishino, Mitsuko, Nakano, Miyako, Miyoshi, Eiji, Suzuki, Kenichi G. N., Kitagawa, Hiroshi, Nakano, Akihiko
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 27.05.2024; Nature Publishing Group; Nature Portfolio
• Subjects: 13/109; 13/44; 13/89; 14/1; 14/19; 14/28; 14/34; 14/35; 631/1647/328/2238; 631/80/313/1525; 631/80/458/1524; 631/80/642/1525; CRISPR; CRISPR-Cas Systems; Enzymes; Glycosaminoglycans; Glycosaminoglycans - metabolism; Glycosylation; Golgi apparatus; Golgi Apparatus - metabolism; Golgi Matrix Proteins; HeLa Cells; Humanities and Social Sciences; Humans; Localization; Membrane Proteins - genetics; Membrane Proteins - metabolism; Microscopy; multidisciplinary; Pathogenesis; Photobleaching; Science; Science (multidisciplinary); Structure-function relationships; Synthesis
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-024-48901-1

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. The structure of the Golgi and the localization of glycosylation enzymes remain largely elusive. Here, the authors use super-resolution microscopy to show that the Golgi is composed of small dynamic units which have rapidly moving zones of glycosylation enzymes.