Titre :

Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes

Auteur(s) :

Toustou, Charlotte [Auteur]
Walet‐Balieu, Marie‐Laure [Auteur]
Kiefer‐Meyer, Marie‐Christine [Auteur]
Houdou, Marine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Catholic University of Leuven = Katholieke Universiteit Leuven [KU Leuven]
Lerouge, Patrice [Auteur]
Foulquier, Francois [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Bardor, Muriel [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Laboratoire de Glycobiologie et Matrice Extracellulaire Végétale [Glyco-MEV]

Titre de la revue :

Biological Reviews

Nom court de la revue :

Biol Rev

Éditeur :

Wiley

Date de publication :

2021-12-06

ISSN :

1464-7931

Mot(s)-clé(s) en anglais :

calcium homeostasis
endoplasmic reticulum
eukaryotes
glycosylation
glycosyltransferases
Golgi apparatus
manganese homeostasis
N-glycans
regulation
structural diversity

Discipline(s) HAL :

Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire

Résumé en anglais : [en]

N-glycosylation is an important post-translational modification of proteins that has been highly conserved during evolution and is found in Eukaryota, Bacteria and Archaea. In eukaryotes, N-glycan processing is sequential, ...
Lire la suite >N-glycosylation is an important post-translational modification of proteins that has been highly conserved during evolution and is found in Eukaryota, Bacteria and Archaea. In eukaryotes, N-glycan processing is sequential, involving multiple specific steps within the secretory pathway as proteins travel through the endoplasmic reticulum and the Golgi apparatus. In this review, we first summarize the different steps of the N-glycan processing and further describe recent findings regarding the diversity of N-glycan structures in eukaryotic clades. This comparison allows us to explore the different regulation mechanisms of N-glycan processing among eukaryotic clades. Recent findings regarding the regulation of protein N-glycosylation are highlighted, especially the regulation of the biosynthesis of complex-type N-glycans through manganese and calcium homeostasis and the specific role of transmembrane protein 165 (TMEM165) for which homologous sequences have been identified in several eukaryotic clades. Further research will be required to characterize the function of TMEM165 homologous sequences in different eukaryotic clades.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

Université de Lille
CNRS

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

Mécanismes moléculaires de la N-glycosylation et pathologies associées

Date de dépôt :

2022-01-21T11:27:09Z
2022-01-21T13:58:15Z