Towards understanding the extensive diversity ...
Document type :
Article dans une revue scientifique: Article original
DOI :
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Title :
Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes
Author(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]
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]
Journal title :
Biological Reviews
Abbreviated title :
Biol Rev
Publisher :
Wiley
Publication date :
2021-12-06
ISSN :
1464-7931
English keyword(s) :
calcium homeostasis
endoplasmic reticulum
eukaryotes
glycosylation
glycosyltransferases
Golgi apparatus
manganese homeostasis
N-glycans
regulation
structural diversity
endoplasmic reticulum
eukaryotes
glycosylation
glycosyltransferases
Golgi apparatus
manganese homeostasis
N-glycans
regulation
structural diversity
HAL domain(s) :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
Chimie/Chimie théorique et/ou physique
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
English abstract : [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, ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
Mécanismes moléculaires de la N-glycosylation et pathologies associées
Submission date :
2022-01-21T11:27:09Z
2022-01-21T13:58:15Z
2022-01-21T13:58:15Z
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