学術雑誌論文

学術雑誌論文

Nature Communications. 2024, 15(1), p. 4514

Dynamic movement of the Golgi unit and its glycosylation enzyme zones

Nature Research

英語

2024-05-27

https://doi.org/10.1038/S41467-024-48901-1

Harada A., Kunii M., Kurokawa K., et al. Dynamic movement of the Golgi unit and its glycosylation enzyme zones. Nature Communications 15, 4514 (2024); https://doi.org/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.

This article is licensed under a Creative Commons Attribution 4.0 International License.

97264

Dynamic movement of the Golgi unit and its glycosylation enzyme zones

Nature Research

英語

2024-05-27

Nature Communications

15

1

4514

https://doi.org/10.1038/S41467-024-48901-1

https://hdl.handle.net/11094/97264