Dynamic movement of the Golgi unit and its glycosylation enzyme zones

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

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

Dynamic movement of the Golgi unit and its glycosylation enzyme zones

Harada, Akihiro; Kunii, Masataka; Kurokawa, Kazuo et al.

Nature Communications, 2024, 15(1), 4514

Number of Access:3,683（2025-07-27 23:30 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/97264

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Title	Dynamic movement of the Golgi unit and its glycosylation enzyme zones
Creator	NRID 1000040251441 1000040251441 researchmap permalink aharada aharada Scopus Author ID 7202253419 7202253419 CreatorName Harada, Akihiro
	NRID 1000080614768 1000080614768 ORCID 0000-0001-7222-7456 0000-0001-7222-7456 researchmap permalink kunimasa kunimasa Scopus Author ID 23985234600 23985234600 CreatorName Kunii, Masataka
	NRID 1000040333504 1000040333504 CreatorName Kurokawa, Kazuo
	NRID 1000080836883 1000080836883 researchmap permalink tsumi tsumi CreatorName Sumi, Takuya
	CreatorName Kanda, Satoshi
	CreatorName Zhang, Yu
	NRID 1000060378578 1000060378578 CreatorName Nadanaka, Satomi
	CreatorName Hirosawa, Koichiro M.
	CreatorName Tokunaga, Kazuaki
	NRID 1000000373332 1000000373332 CreatorName Tojima, Takuro
	NRID 1000030397707 1000030397707 researchmap permalink manabutaniguchi manabutaniguchi CreatorName Taniguchi, Manabu
	CreatorName Moriwaki, Kenta
	NRID 1000060584521 1000060584521 researchmap permalink sw-510119 sw-510119 Scopus Author ID 35598338400 35598338400 CreatorName Yoshimura, Shin-Ichiro
	NRID 1000040301783 1000040301783 CreatorName Yamamoto-Hino, Miki
	NRID 1000060280575 1000060280575 CreatorName Goto, Satoshi
	NRID 1000060291895 1000060291895 CreatorName Katagiri, Toyomasa
	NRID 1000030708441 1000030708441 CreatorName Kume, Satoshi
	NRID 1000030510440 1000030510440 researchmap permalink mitsuko mitsuko Scopus Author ID 25937253600 25937253600 CreatorName Hayashi-Nishino, Mitsuko
	NRID 1000040397724 1000040397724 CreatorName Nakano, Miyako
	NRID 1000020322183 1000020322183 ORCID 0000-0002-9430-2362 0000-0002-9430-2362 researchmap permalink read0068532 read0068532 Scopus Author ID 7005784183 7005784183 CreatorName Miyoshi, Eiji
	NRID 1000050423059 1000050423059 CreatorName Suzuki, Kenichi G.N.
	NRID 1000040221915 1000040221915 CreatorName Kitagawa, Hiroshi
	NRID 1000090142140 1000090142140 CreatorName Nakano, Akihiko
Description	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.
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.
Publisher	Nature Research
Source Title	Nature Communications
Volume (Issue)	15(1)
Page	4514
Date of Issued	2024-05-27
Language	English
Handle URL	https://hdl.handle.net/11094/97264
eISSN	20411723
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1038/S41467-024-48901-1
Access Rights	open access
CopyRight	This article is licensed under a Creative Commons Attribution 4.0 International License.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCTERMS.bibliographicCitation	Nature Communications. 2024, 15(1), p. 4514
DC.title	Dynamic movement of the Golgi unit and its glycosylation enzyme zones
DC.creator	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
DC.publisher	Nature Research
DC.language' scheme='DCTERMS.RFC1766	English
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2024-05-27
DC.identifier	https://doi.org/10.1038/S41467-024-48901-1
DC.description	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.
DCTERMS.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.
DC.rights	This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	97264
citation_title	Dynamic movement of the Golgi unit and its glycosylation enzyme zones
citation_author	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
citation_publisher	Nature Research
citation_language	English
citation_date	2024-05-27
citation_journal_title	Nature Communications
citation_volume	15
citation_issue	1
citation_firstpage	4514
citation_doi	https://doi.org/10.1038/S41467-024-48901-1
citation_public_url	https://hdl.handle.net/11094/97264

Dynamic movement of the Golgi unit and its glycosylation enzyme zones

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