Evidence map›Paper›PMID 38802491›Full record

ArticleNature communications2024

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 and 13 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Golgi Units as Modules in the Ribbon.Sub-cellular biochemistry · 2026
    Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. GalNAc-Transferases in Cancer.Biomedicines · 2025
    Review
  14. Quantitative Modeling of IgG N-Glycosylation Profiles from Population Data.International journal of molecular sciences · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025
    Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

23 authors.

Akihiro Harada *Department of Cell Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan. aharada@acb.med.osaka-u.ac.jp.ORCID http://orcid.org/0000-0002-2484-9784
Masataka Kunii *Department of Cell Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Kazuo Kurokawa *Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, Wako, Saitama, Japan.ORCID http://orcid.org/0000-0003-3549-4795
Takuya Sumi *Department of Cell Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.ORCID http://orcid.org/0000-0001-6994-2926
Satoshi KandaDepartment of Cell Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Yu ZhangDepartment of Cell Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Satomi NadanakaLaboratory of Biochemistry, Kobe Pharmaceutical University, Kobe, Hyogo, Japan.ORCID http://orcid.org/0000-0001-7650-836X
Koichiro M HirosawaLaboratory of Cell Biophysics, Institute for Glyco-core Research (iGCORE), Gifu University, Gifu, Gifu, Japan.ORCID http://orcid.org/0000-0003-0170-3755
Kazuaki TokunagaNIKON SOLUTIONS CO., LTD., Tokyo, Japan.
Takuro TojimaLive Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, Wako, Saitama, Japan.ORCID http://orcid.org/0000-0002-9140-3205
Manabu TaniguchiDepartment of Cell Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Kenta MoriwakiDepartment of Cell Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.ORCID http://orcid.org/0000-0002-8724-4715
Shin-Ichiro YoshimuraDepartment of Cell Biology, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Miki Yamamoto-HinoDepartment of Life Science, Rikkyo University, Toshima-ku, Tokyo, Japan.
Satoshi GotoDepartment of Life Science, Rikkyo University, Toshima-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0002-1805-4766
Toyomasa KatagiriLaboratory of Biofunctional Molecular Medicine, National Institute of Biomedical Innovation, National Institutes of Biomedical Innovation, Health and Nutrition, Ibaraki, Osaka, Japan.
Satoshi KumeLaboratory for Pathophysiological and Health Science, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan.ORCID http://orcid.org/0000-0001-7481-2843
Mitsuko Hayashi-NishinoSANKEN (The Institute of Scientific and Industrial Research), Osaka University, Ibaraki, Osaka, Japan.
Miyako NakanoGraduate School of Integrated Sciences for Life, Hiroshima University, Higashi-Hiroshima, Hiroshima, Japan.
Eiji MiyoshiDepartment of Molecular Biochemistry and Clinical Investigation, Osaka University Graduate School of Medicine, Suita, Osaka, Japan.ORCID http://orcid.org/0000-0002-9430-2362
Kenichi G N SuzukiLaboratory of Cell Biophysics, Institute for Glyco-core Research (iGCORE), Gifu University, Gifu, Gifu, Japan.ORCID http://orcid.org/0000-0002-8436-5757
Hiroshi KitagawaLaboratory of Biochemistry, Kobe Pharmaceutical University, Kobe, Hyogo, Japan.ORCID http://orcid.org/0000-0002-9307-7079
Akihiko NakanoLive Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, Wako, Saitama, Japan.ORCID http://orcid.org/0000-0003-3635-548X

Funding

Ministry of Education, Culture, Sports, Science and Technology (MEXT) 17H0622Ministry of Education, Culture, Sports, Science and Technology (MEXT) 17H06413Ministry of Education, Culture, Sports, Science and Technology (MEXT) 17H06420Ministry of Education, Culture, Sports, Science and Technology (MEXT) 18H05275Ministry of Education, Culture, Sports, Science and Technology (MEXT) 21H02658Ministry of Education, Culture, Sports, Science and Technology (MEXT) 21K06734
6 · The paper itself

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.

Indexed as

GlycosaminoglycansGolgi ApparatusCRISPR-Cas SystemsGlycosylationGolgi Matrix ProteinsHeLa CellsHumansMembrane ProteinsGlycosaminoglycansGolgi Matrix ProteinsmacrogolginMembrane Proteins

Identifiers

PMID38802491
PMCPMC11130159

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.