Biometals and glycosylation in humans: ...
Type de document :
Article dans une revue scientifique
URL permanente :
Titre :
Biometals and glycosylation in humans: Congenital disorders of glycosylation shed lights into the crucial role of Golgi manganese homeostasis
Auteur(s) :
Foulquier, Francois [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Legrand, Dominique [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Legrand, Dominique [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Titre de la revue :
Biochimica et Biophysica Acta (BBA) - General Subjects
Nom court de la revue :
Biochimica et Biophysica Acta (BBA) - General Subjects
Numéro :
1864
Pagination :
129674
Éditeur :
Elsevier BV
Date de publication :
2020-10
ISSN :
0304-4165
Mot(s)-clé(s) en anglais :
Glycosylation
Congenital disorders of glycosylation
Biometal homeostasis
Manganese
TMEM165
Congenital disorders of glycosylation
Biometal homeostasis
Manganese
TMEM165
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Mécanismes moléculaires de la N-glycosylation et pathologies associées
Date de dépôt :
2021-03-23T15:00:40Z
2021-03-24T07:15:57Z
2021-03-24T07:15:57Z
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