Title :

The vertebrate sialylation machinery: structure-function and molecular evolution of GT-29 sialyltransferases

Author(s) :

Harduin-Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Journal title :

Glycoconjugate Journal

Abbreviated title :

Glycoconj J

Volume number :

40

Pages :

473-492

Publisher :

Springer Verlag

Publication date :

2023-05-29

ISSN :

0282-0080

English keyword(s) :

Sialic acid
Sialyltransferase
Structure-function
Evolution
Enzyme activity

HAL domain(s) :

Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique

English abstract : [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 ...
Show more >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.Show less >

Language :

Anglais

Audience :

Internationale

Popular science :

Non

ANR Project :

Des polysialyltransférases d'origine marine pour la synthèse de bioconjugués immunomodulateurs

Administrative institution(s) :

Université de Lille
CNRS

Collections :

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

Research team(s) :

Régulation de la glycosylation terminale

Submission date :

2023-09-26T13:08:49Z
2023-09-28T12:31:19Z