Evidence map›Paper›PMID 31544102›Full record

ArticleFrontiers in cell and developmental biology2019

The Golgin Protein Giantin Regulates Interconnections Between Golgi Stacks.

Ayano Satoh, Mitsuko Hayashi-Nishino, Takuto Shakuno, Junko Masuda, Mayuko Koreishi, Runa Murakami, Yoshimasa Nakamura, Toshiyuki Nakamura, Naomi Abe-Kanoh, Yasuko Honjo and 3 more

Abstract read
In one paragraph

Article in Frontiers in cell and developmental biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Nanoscale Mapping of the Subcellular Glycosylation Landscape.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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

13 authors.

Ayano SatohGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
Mitsuko Hayashi-NishinoInstitute of Scientific and Industrial Research, Osaka University, Osaka, Japan.
Takuto ShakunoGraduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Junko MasudaGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
Mayuko KoreishiGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
Runa MurakamiGraduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
Yoshimasa NakamuraGraduate School of Environmental and Life Science, Okayama University, Okayama, Japan.
Toshiyuki NakamuraGraduate School of Environmental and Life Science, Okayama University, Okayama, Japan.
Naomi Abe-KanohGraduate School of Environmental and Life Science, Okayama University, Okayama, Japan.
Yasuko HonjoResearch Institute for Radiation Biology and Medicine, Hiroshima University, Hiroshima, Japan.
Joerg MalsamCenter for Biochemistry (BZH), Heidelberg University, Heidelberg, Germany.
Sidney YuSchool of Biomedical Sciences, The Chinese University of Hong Kong, Hong Kong, Hong Kong.
Kunihiko NishinoInstitute of Scientific and Industrial Research, Osaka University, Osaka, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Golgins are a family of Golgi-localized long coiled-coil proteins. The major golgin function is thought to be the tethering of vesicles, membranes, and cytoskeletal elements to the Golgi. We previously showed that knockdown of one of the longest golgins, Giantin, altered the glycosylation patterns of cell surfaces and the kinetics of cargo transport, suggesting that Giantin maintains correct glycosylation through slowing down transport within the Golgi. Giantin knockdown also altered the sizes and numbers of mini Golgi stacks generated by microtubule de-polymerization, suggesting that it maintains the independence of individual Golgi stacks. Therefore, it is presumed that Golgi stacks lose their independence following Giantin knockdown, allowing easier and possibly increased transport among stacks and abnormal glycosylation. To gain structural insights into the independence of Golgi stacks, we herein performed electron tomography and 3D modeling of Golgi stacks in Giantin knockdown cells. Compared with control cells, Giantin-knockdown cells had fewer and smaller fenestrae within each cisterna. This was supported by data showing that the diffusion rate of Golgi membrane proteins is faster in Giantin-knockdown Golgi, indicating that Giantin knockdown structurally and functionally increases connectivity among Golgi cisternae and stacks. This increased connectivity suggests that contrary to the

Indexed as

electron tomographyendoplasmic reticulumglycosylationGolgigolgins

Identifiers

PMID31544102
PMCPMC6732663

What OpenQuestion holds

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Registered trials

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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 OpenQuestion graph.