Evidence map›Paper›PMID 39779512›Full record

ArticleCellular and molecular life sciences : CMLS2025

SLC10A7 regulates O-GalNAc glycosylation and Ca

Zoé Durin, Aurore Layotte, Willy Morelle, Marine Houdou, Antoine Folcher, Dominique Legrand, Dirk Lefeber, Natalia Prevarskaya, Julia Von Blume, Valérie Cormier-Daire and 1 more

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In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

11 authors.

Zoé DurinUniv. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale Et Fonctionnelle, 59000, Lille, France.
Aurore LayotteUniv. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale Et Fonctionnelle, 59000, Lille, France.
Willy MorelleUniv. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale Et Fonctionnelle, 59000, Lille, France.
Marine HoudouUniv. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale Et Fonctionnelle, 59000, Lille, France.
Antoine FolcherInserm U1003, Laboratory of Excellence, Ion Channels Science and Therapeutics, Equipe Labellisée Par La Ligue Nationale Contre Le Cancer, GIS ONCO Lille, University of Lille, Lille, France.
Dominique LegrandUniv. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale Et Fonctionnelle, 59000, Lille, France.
Dirk LefeberDepartment of Neurology, Donders Institute for Brain, Cognition and Behavior, Radboud University Medical Center, 6525 GA, Nijmegen, The Netherlands.
Natalia PrevarskayaInserm U1003, Laboratory of Excellence, Ion Channels Science and Therapeutics, Equipe Labellisée Par La Ligue Nationale Contre Le Cancer, GIS ONCO Lille, University of Lille, Lille, France.
Julia Von BlumeDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Valérie Cormier-DaireINSERM UMR1163, Institut Imagine, Université de Paris, Paris, France.
François FoulquierUniv. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale Et Fonctionnelle, 59000, Lille, France. francois.foulquier@univ-lille.fr.ORCID http://orcid.org/0009-0000-0219-0862

Funding

Agence Nationale de la Recherche ANR-18-CE14-0040
6 · The paper itself

Abstract

Glycans are known to be fundamental for many cellular and physiological functions. Congenital disorders of glycosylation (CDG) currently encompassing over 160 subtypes, are characterized by glycan synthesis and/or processing defects. Despite the increasing number of CDG patients, therapeutic options remain very limited as our knowledge on glycan synthesis is fragmented. The emergence of CDG resulting from defects in ER/ Golgi homeostasis makes this even more difficult. SLC10A7 belongs to the SLC10 protein family, known as bile acid and steroid transport family, exhibiting a unique structure. It shows a ubiquitous expression and is linked to negative calcium regulation in cells. The mechanisms by which SLC10A7 deficiency leads to Golgi glycosylation abnormalities are unknown. The present study identifies major O-glycosylation defects in both SLC10A7 KO HAP1 cells and SLC10A7-CDG patient fibroblasts and reveals an increased ER and Golgi calcium contents. We also show that the abundance of COSMC and C1GALT1 is altered in SLC10A7-CDG patient cells, as well as the subcellular Golgi localization of the Ca

Indexed as

CalciumCongenital Disorders of GlycosylationGolgi ApparatusHomeostasisAntiportersCalcium-Binding ProteinsEndoplasmic ReticulumFibroblastsGlycosylationHumansManganeseOrganic Anion Transporters, Sodium-DependentSecretory PathwaySymportersAntiportersCalciumCalcium-Binding ProteinsManganeseOrganic Anion Transporters, Sodium-Dependentsodium-bile acid cotransporterSymportersCDGGlycosylationO-GalNAcSLC10A7

Identifiers

PMID39779512
PMCPMC11711720

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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.