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Article ; Online: Metalloglycobiology: The power of metals in regulating glycosylation.

Durin, Zoé / Houdou, Marine / Legrand, Dominique / Foulquier, François

Biochimica et biophysica acta. General subjects

2023 Volume 1867, Issue 9, Page(s) 130412

Abstract: The remarkable structural diversity of glycans that is exposed at the cell surface and generated along the secretory pathway is tightly regulated by several factors. The recent identification of human glycosylation diseases related to metal transporter ... ...

Abstract	The remarkable structural diversity of glycans that is exposed at the cell surface and generated along the secretory pathway is tightly regulated by several factors. The recent identification of human glycosylation diseases related to metal transporter defects opened a completely new field of investigation, referred to herein as "metalloglycobiology", on how metal changes can affect the glycosylation and hence the glycan structures that are produced. Although this field is in its infancy, this review aims to go through the different glycosylation steps/pathways that are metal dependent and that could be impacted by metal homeostasis dysregulations.
MeSH term(s)	Humans ; Cation Transport Proteins/metabolism ; Congenital Disorders of Glycosylation/metabolism ; Endoplasmic Reticulum/enzymology ; Endoplasmic Reticulum/metabolism ; Glycomics/trends ; Glycosylation ; Golgi Apparatus/enzymology ; Golgi Apparatus/metabolism ; Homeostasis ; Magnesium/chemistry ; Magnesium/metabolism ; Metals/chemistry ; Metals/metabolism ; Oxidation-Reduction ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Zinc/chemistry ; Zinc/metabolism
Chemical Substances	Cation Transport Proteins ; Magnesium (I38ZP9992A) ; Metals ; Polysaccharides ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2023-06-20
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2023.130412
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Article ; Online: Metalloglycobiology: The power of metals in regulating glycosylation

Durin, Zoé / Houdou, Marine / Legrand, Dominique / Foulquier, François

BBA - General Subjects. 2023 Sept., v. 1867, no. 9 p.130412-

2023

Abstract	The remarkable structural diversity of glycans that is exposed at the cell surface and generated along the secretory pathway is tightly regulated by several factors. The recent identification of human glycosylation diseases related to metal transporter defects opened a completely new field of investigation, referred to herein as “metalloglycobiology”, on how metal changes can affect the glycosylation and hence the glycan structures that are produced. Although this field is in its infancy, this review aims to go through the different glycosylation steps/pathways that are metal dependent and that could be impacted by metal homeostasis dysregulations.
Keywords	glycosylation ; homeostasis ; humans ; polysaccharides ; Metals ; Regulation ; CDG
Language	English
Dates of publication	2023-09
Publishing place	Elsevier B.V.
Document type	Article ; Online
ZDB-ID	840755-1
ISSN	0304-4165
ISSN	0304-4165
DOI	10.1016/j.bbagen.2023.130412
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Article ; Online: Anomalies congénitales de la glycosylation (CDG) - 1980-2020, 40 ans pour comprendre.

Houdou, Marine / Foulquier, François

Medecine sciences : M/S

2020 Volume 36, Issue 8-9, Page(s) 735–746

Abstract: Glycosylation is an essential and complex cellular process where monosaccharides are added one by one onto an acceptor molecule, most of the time a protein or a lipid, so called glycoprotein or glycolipid. This cellular process is found in every living ... ...

Title translation	Panorama on congenital disorders of glycosylation (CDG): from 1980 to 2020.
Abstract	Glycosylation is an essential and complex cellular process where monosaccharides are added one by one onto an acceptor molecule, most of the time a protein or a lipid, so called glycoprotein or glycolipid. This cellular process is found in every living organism and is tightly conserved during evolution. In human, if one of the glycosylation reactions is genetically impaired, Congenital Disorders of Glycosylation (CDG) appear. CDG are a growing family of more than a hundred genetic diseases. This review offers a panorama of CDGs from 1980 to the present, their discoveries, diagnoses and treatments.
MeSH term(s)	Animals ; Congenital Disorders of Glycosylation/diagnosis ; Congenital Disorders of Glycosylation/epidemiology ; Congenital Disorders of Glycosylation/genetics ; Congenital Disorders of Glycosylation/therapy ; Genetic Association Studies/history ; Genetic Association Studies/trends ; Genetic Testing/history ; Genetic Testing/methods ; Genetic Testing/trends ; Glycosylation ; History, 20th Century ; History, 21st Century ; Humans
Language	French
Publishing date	2020-08-21
Publishing country	France
Document type	Historical Article ; Journal Article ; Review
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2020128
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Article ; Online: Biometals and glycosylation in humans: Congenital disorders of glycosylation shed lights into the crucial role of Golgi manganese homeostasis.

Foulquier, François / Legrand, Dominique

Biochimica et biophysica acta. General subjects

2020 Volume 1864, Issue 10, Page(s) 129674

Abstract: About half of the eukaryotic proteins bind biometals that participate in their structure and functions in virtually all physiological processes, including glycosylation. After reviewing the biological roles and transport mechanisms of calcium, magnesium, ...

Abstract	About half of the eukaryotic proteins bind biometals that participate in their structure and functions in virtually all physiological processes, including glycosylation. After reviewing the biological roles and transport mechanisms of calcium, magnesium, manganese, zinc and cobalt acting as cofactors of the metalloproteins involved in sugar metabolism and/or glycosylation, the paper will outline the pathologies resulting from a dysregulation of these metals homeostasis and more particularly Congenital Disorders of Glycosylation (CDGs) caused by ion transporter defects. Highlighting of CDGs due to defects in SLC39A8 (ZIP8) and TMEM165, two proteins transporting manganese from the extracellular space to cytosol and from cytosol to the Golgi lumen, respectively, has emphasized the importance of manganese homeostasis for glycosylation. Based on our current knowledge of TMEM165 structure and functions, this review will draw a picture of known and putative mechanisms regulating manganese homeostasis in the secretory pathway.
MeSH term(s)	Animals ; Antiporters/metabolism ; Biological Transport ; Cation Transport Proteins/metabolism ; Congenital Disorders of Glycosylation/metabolism ; Congenital Disorders of Glycosylation/pathology ; Glycosylation ; Golgi Apparatus/metabolism ; Golgi Apparatus/pathology ; Homeostasis ; Humans ; Manganese/metabolism
Chemical Substances	Antiporters ; Cation Transport Proteins ; SLC39A8 protein, human ; TMEM165 protein, human ; Manganese (42Z2K6ZL8P)
Language	English
Publishing date	2020-06-26
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2020.129674
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Article: Biometals and glycosylation in humans: Congenital disorders of glycosylation shed lights into the crucial role of Golgi manganese homeostasis

Foulquier, François / Legrand, Dominique

Biochimica et biophysica acta. 2020 Oct., v. 1864, no. 10

2020

Abstract	About half of the eukaryotic proteins bind biometals that participate in their structure and functions in virtually all physiological processes, including glycosylation. After reviewing the biological roles and transport mechanisms of calcium, magnesium, manganese, zinc and cobalt acting as cofactors of the metalloproteins involved in sugar metabolism and/or glycosylation, the paper will outline the pathologies resulting from a dysregulation of these metals homeostasis and more particularly Congenital Disorders of Glycosylation (CDGs) caused by ion transporter defects. Highlighting of CDGs due to defects in SLC39A8 (ZIP8) and TMEM165, two proteins transporting manganese from the extracellular space to cytosol and from cytosol to the Golgi lumen, respectively, has emphasized the importance of manganese homeostasis for glycosylation. Based on our current knowledge of TMEM165 structure and functions, this review will draw a picture of known and putative mechanisms regulating manganese homeostasis in the secretory pathway.
Keywords	calcium ; cobalt ; congenital abnormalities ; cytosol ; extracellular space ; glycosylation ; homeostasis ; humans ; magnesium ; manganese ; metalloproteins ; sugars ; zinc
Language	English
Dates of publication	2020-10
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	840755-1
ISSN	0304-4165
ISSN	0304-4165
DOI	10.1016/j.bbagen.2020.129674
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Article ; Online: TMEM165 a new player in proteoglycan synthesis: loss of TMEM165 impairs elongation of chondroitin- and heparan-sulfate glycosaminoglycan chains of proteoglycans and triggers early chondrocyte differentiation and hypertrophy.

Khan, Sajida / Sbeity, Malak / Foulquier, François / Barré, Lydia / Ouzzine, Mohamed

Cell death & disease

2021 Volume 13, Issue 1, Page(s) 11

Abstract: TMEM165 deficiency leads to skeletal disorder characterized by major skeletal dysplasia and pronounced dwarfism. However, the molecular mechanisms involved have not been fully understood. Here, we uncover that TMEM165 deficiency impairs the synthesis of ... ...

Abstract	TMEM165 deficiency leads to skeletal disorder characterized by major skeletal dysplasia and pronounced dwarfism. However, the molecular mechanisms involved have not been fully understood. Here, we uncover that TMEM165 deficiency impairs the synthesis of proteoglycans by producing a blockage in the elongation of chondroitin-and heparan-sulfate glycosaminoglycan chains leading to the synthesis of proteoglycans with shorter glycosaminoglycan chains. We demonstrated that the blockage in elongation of glycosaminoglycan chains is not due to defect in the Golgi elongating enzymes but rather to availability of the co-factor Mn
MeSH term(s)	Animals ; Antiporters/deficiency ; Antiporters/genetics ; Antiporters/metabolism ; Case-Control Studies ; Cation Transport Proteins/deficiency ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Cell Differentiation/genetics ; Cell Line, Tumor ; Chondrocytes/metabolism ; Chondrocytes/pathology ; Chondrogenesis/genetics ; Chondroitin Sulfates/biosynthesis ; Dwarfism/metabolism ; Dwarfism/pathology ; Fibroblasts/metabolism ; Gene Knockout Techniques/methods ; Glycosylation ; HEK293 Cells ; Heparan Sulfate Proteoglycans/biosynthesis ; Humans ; Hypertrophy/metabolism ; Mice ; Signal Transduction/genetics ; Transfection
Chemical Substances	Antiporters ; Cation Transport Proteins ; Heparan Sulfate Proteoglycans ; TMEM165 protein, human ; TMEM165 protein, mouse ; Chondroitin Sulfates (9007-28-7)
Language	English
Publishing date	2021-12-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-021-04458-1
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Article: Variation of the serum

Lebredonchel, Elodie / Duvet, Sandrine / Douillard, Claire / Foulquier, François / Klein, André

JIMD reports

2021 Volume 62, Issue 1, Page(s) 22–29

Abstract: For the first time the glycosylation of a patient with a MPI-CDG during pregnancy is monitored. MPI-CDG, is characterised by a deficiency in mannose-6-phosphate isomerase (MPI) leading to a reduced pool of glycosylation precursors, impairing the ... ...

Abstract	For the first time the glycosylation of a patient with a MPI-CDG during pregnancy is monitored. MPI-CDG, is characterised by a deficiency in mannose-6-phosphate isomerase (MPI) leading to a reduced pool of glycosylation precursors, impairing the biosynthesis of
Language	English
Publishing date	2021-09-17
Publishing country	United States
Document type	Case Reports
ZDB-ID	2672872-2
ISSN	2192-8312 ; 2192-8304
ISSN (online)	2192-8312
ISSN	2192-8304
DOI	10.1002/jmd2.12247
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Article ; Online: Les mécanismes de régulation de la glycosylation - Exemples d’altérations des chaînes glycanniques dans les cancers.

Groux-Degroote, Sophie / Foulquier, François / Cavdarli, Sumeyye / Delannoy, Philippe

Medecine sciences : M/S

2021 Volume 37, Issue 6-7, Page(s) 609–617

Abstract: Glycosylation is one of the essential modifications of proteins and lipids. It is carried out mainly in the endoplasmic reticulum and Golgi apparatus, and requires a specific molecular machinery associating several hundreds of glycosyltransferases, ... ...

Title translation	Reticular and Golgi glycosylation: Advances and associated diseases.
Abstract	Glycosylation is one of the essential modifications of proteins and lipids. It is carried out mainly in the endoplasmic reticulum and Golgi apparatus, and requires a specific molecular machinery associating several hundreds of glycosyltransferases, glycosidases, transporters and regulating proteins. Modifications of glycosylation are found in numerous diseases, notably in cancers. All types of glycosylation can be affected and this leads to dysfunctions of cellular metabolism. In this review, we present the current knowledge on the regulation of glycosylation mechanisms and illustrate how the alteration of these regulatory mechanisms can lead to abnormal protein and lipid glycosylation, and take part in the development of cancers.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Glycosylation ; Glycosyltransferases/genetics ; Golgi Apparatus ; Humans
Chemical Substances	Glycosyltransferases (EC 2.4.-)
Language	French
Publishing date	2021-06-28
Publishing country	France
Document type	Journal Article ; Review
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2021082
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Article ; Online: SLC10A7, an orphan member of the SLC10 family involved in congenital disorders of glycosylation.

Durin, Zoé / Dubail, Johanne / Layotte, Aurore / Legrand, Dominique / Cormier-Daire, Valérie / Foulquier, François

Human genetics

2022 Volume 141, Issue 7, Page(s) 1287–1298

Abstract: SLC10A7, encoded by the so-called SLC10A7 gene, is the seventh member of a human sodium/bile acid cotransporter family, known as the SLC10 family. Despite similarities with the other members of the SLC10 family, SLC10A7 does not exhibit any transport ... ...

Abstract	SLC10A7, encoded by the so-called SLC10A7 gene, is the seventh member of a human sodium/bile acid cotransporter family, known as the SLC10 family. Despite similarities with the other members of the SLC10 family, SLC10A7 does not exhibit any transport activity for the typical SLC10 substrates and is then considered yet as an orphan carrier. Recently, SLC10A7 mutations have been identified as responsible for a new Congenital Disorder of Glycosylation (CDG). CDG are a family of rare and inherited metabolic disorders, where glycosylation abnormalities lead to multisystemic defects. SLC10A7-CDG patients presented skeletal dysplasia with multiple large joint dislocations, short stature and amelogenesis imperfecta likely mediated by glycosaminoglycan (GAG) defects. Although it has been demonstrated that the transporter and substrate specificities of SLC10A7, if any, differ from those of the main members of the protein family, SLC10A7 seems to play a role in Ca
MeSH term(s)	Amelogenesis Imperfecta ; Congenital Disorders of Glycosylation/genetics ; Glycosaminoglycans/genetics ; Glycosylation ; Humans ; Organic Anion Transporters, Sodium-Dependent ; Osteochondrodysplasias ; Symporters
Chemical Substances	Glycosaminoglycans ; Organic Anion Transporters, Sodium-Dependent ; Slc10a7 protein, human ; Symporters
Language	English
Publishing date	2022-01-08
Publishing country	Germany
Document type	Journal Article
ZDB-ID	223009-4
ISSN	1432-1203 ; 0340-6717
ISSN (online)	1432-1203
ISSN	0340-6717
DOI	10.1007/s00439-021-02420-x
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Article: New insights into the pathogenicity of TMEM165 variants using structural modeling based on AlphaFold 2 predictions.

Legrand, Dominique / Herbaut, Mélissandre / Durin, Zoé / Brysbaert, Guillaume / Bardor, Muriel / Lensink, Marc F / Foulquier, François

Computational and structural biotechnology journal

2023 Volume 21, Page(s) 3424–3436

Abstract: TMEM165 is a Golgi protein playing a crucial role in ... ...

Abstract	TMEM165 is a Golgi protein playing a crucial role in Mn
Language	English
Publishing date	2023-06-17
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2694435-2
ISSN	2001-0370
ISSN	2001-0370
DOI	10.1016/j.csbj.2023.06.015
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