Evidence map›Paper›PMID 29093022›Full record

ArticleJournal of cell science2017

Giantin-knockout models reveal a feedback loop between Golgi function and glycosyltransferase expression.

Nicola L Stevenson, Dylan J M Bergen, Roderick E H Skinner, Erika Kague, Elizabeth Martin-Silverstone, Kate A Robson Brown, Chrissy L Hammond, David J Stephens

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
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

40 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. [Research progress on collagen secretion mechanisms in scarring].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2025
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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

8 authors at 1 institution in 1 country.

Nicola L StevensonCell Biology Laboratories, School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.ORCID http://orcid.org/0000-0001-8967-7277
Dylan J M BergenCell Biology Laboratories, School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.ORCID http://orcid.org/0000-0001-7808-6121
Roderick E H SkinnerSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Erika KagueSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.ORCID http://orcid.org/0000-0002-0266-9424
Elizabeth Martin-SilverstoneSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.ORCID http://orcid.org/0000-0003-0139-2109
Kate A Robson BrownComputed Tomography Laboratory, School of Arts, University of Bristol, 43 Woodland Road, Bristol BS8 1UU, UK.ORCID http://orcid.org/0000-0003-4797-8965
Chrissy L HammondSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK.ORCID http://orcid.org/0000-0002-4935-6724
David J StephensCell Biology Laboratories, School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, UK david.stephens@bristol.ac.uk.ORCID http://orcid.org/0000-0001-5297-3240
University of Bristol · GB

Funding

Arthritis Research UK 19476Medical Research Council MR/K018019/1Medical Research Council MR/P000177/1Wellcome Trust
6 · The paper itself

Abstract

The Golgi is the cellular hub for complex glycosylation, controlling accurate processing of complex proteoglycans, receptors, ligands and glycolipids. Its structure and organisation are dependent on golgins, which tether cisternal membranes and incoming transport vesicles. Here, we show that knockout of the largest golgin, giantin, leads to substantial changes in gene expression but only limited effects on Golgi structure. Notably, 22 Golgi-resident glycosyltransferases, but not glycan-processing enzymes or the ER glycosylation machinery, are differentially expressed following giantin ablation. This includes near-complete loss of function of GALNT3 in both mammalian cell and zebrafish models. Giantin-knockout zebrafish exhibit hyperostosis and ectopic calcium deposits, recapitulating phenotypes of hyperphosphatemic familial tumoral calcinosis, a disease caused by mutations in GALNT3. These data reveal a new feature of Golgi homeostasis: the ability to regulate glycosyltransferase expression to generate a functional proteoglycome.

Indexed as

AnimalsCell LineGene Expression Regulation, EnzymologicGlycosyltransferasesGolgi ApparatusGolgi Matrix ProteinsHumansMembrane ProteinsMutationN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseZebrafishGlycosyltransferasesGolgi Matrix ProteinsmacrogolginMembrane ProteinsN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseGALNT3GiantinGlycosylationGolgiHyperphosphatemic tumoral calcinosisZebrafish

Identifiers

PMID29093022
PMCPMC5769581
OpenAlexW2766136641

What OpenQuestion 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 OpenQuestion graph.