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Dynamic movement of the Golgi unit and its glycosylation enzyme zones.

Authors :
Harada A
Kunii M
Kurokawa K
Sumi T
Kanda S
Zhang Y
Nadanaka S
Hirosawa KM
Tokunaga K
Tojima T
Taniguchi M
Moriwaki K
Yoshimura SI
Yamamoto-Hino M
Goto S
Katagiri T
Kume S
Hayashi-Nishino M
Nakano M
Miyoshi E
Suzuki KGN
Kitagawa H
Nakano A
Source :
Nature communications [Nat Commun] 2024 May 27; Vol. 15 (1), pp. 4514. Date of Electronic Publication: 2024 May 27.
Publication Year :
2024

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.<br /> (© 2024. The Author(s).)

Details

Language :
English
ISSN :
2041-1723
Volume :
15
Issue :
1
Database :
MEDLINE
Journal :
Nature communications
Publication Type :
Academic Journal
Accession number :
38802491
Full Text :
https://doi.org/10.1038/s41467-024-48901-1