The vertebrate sialylation machinery: ...
Type de document :
Article dans une revue scientifique: Article de synthèse/Review paper
URL permanente :
Titre :
The vertebrate sialylation machinery: structure-function and molecular evolution of GT-29 sialyltransferases
Auteur(s) :
Titre de la revue :
Glycoconjugate Journal
Nom court de la revue :
Glycoconj J
Numéro :
40
Pagination :
473-492
Éditeur :
Springer Verlag
Date de publication :
2023-05-29
ISSN :
0282-0080
Mot(s)-clé(s) en anglais :
Sialic acid
Sialyltransferase
Structure-function
Evolution
Enzyme activity
Sialyltransferase
Structure-function
Evolution
Enzyme activity
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Every eukaryotic cell is covered with a thick layer of complex carbohydrates with essential roles in their social life. In Deuterostoma, sialic acids present at the outermost positions of glycans of glycoconjugates are ...
Lire la suite >Every eukaryotic cell is covered with a thick layer of complex carbohydrates with essential roles in their social life. In Deuterostoma, sialic acids present at the outermost positions of glycans of glycoconjugates are known to be key players in cellular interactions including host-pathogen interactions. Their negative charge and hydrophilic properties enable their roles in various normal and pathological states and their expression is altered in many diseases including cancers. Sialylation of glycoproteins and glycolipids is orchestrated by the regulated expression of twenty sialyltransferases in human tissues with distinct enzymatic characteristics and preferences for substrates and linkages formed. However, still very little is known on the functional organization of sialyltransferases in the Golgi apparatus and how the sialylation machinery is finely regulated to provide the ad hoc sialome to the cell. This review summarizes current knowledge on sialyltransferases, their structure–function relationships, molecular evolution, and their implications in human biology.Lire moins >
Lire la suite >Every eukaryotic cell is covered with a thick layer of complex carbohydrates with essential roles in their social life. In Deuterostoma, sialic acids present at the outermost positions of glycans of glycoconjugates are known to be key players in cellular interactions including host-pathogen interactions. Their negative charge and hydrophilic properties enable their roles in various normal and pathological states and their expression is altered in many diseases including cancers. Sialylation of glycoproteins and glycolipids is orchestrated by the regulated expression of twenty sialyltransferases in human tissues with distinct enzymatic characteristics and preferences for substrates and linkages formed. However, still very little is known on the functional organization of sialyltransferases in the Golgi apparatus and how the sialylation machinery is finely regulated to provide the ad hoc sialome to the cell. This review summarizes current knowledge on sialyltransferases, their structure–function relationships, molecular evolution, and their implications in human biology.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Projet ANR :
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Régulation de la glycosylation terminale
Date de dépôt :
2023-09-26T13:08:49Z
2023-09-28T12:31:19Z
2023-09-28T12:31:19Z
Fichiers
- P23.26 Harduin-Lepers-2023-Glycoconjugate_Journal.pdf
- Version éditeur
- Accès libre
- Accéder au document