OGT: a short overview of an enzyme standing ...
Document type :
Article dans une revue scientifique
DOI :
PMID :
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Title :
OGT: a short overview of an enzyme standing out from usual glycosyltransferases
Author(s) :
Aquino-Gil, Moyira Osny [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Universidad Nacional Autónoma de México = National Autonomous University of Mexico [UNAM]
Pierce, Annick [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Perez-Cervera, Yobana [Auteur]
Universidad Nacional Autónoma de México = National Autonomous University of Mexico [UNAM]
Zenteno, Edgar [Auteur]
Universidad Nacional Autónoma de México = National Autonomous University of Mexico [UNAM]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Universidad Nacional Autónoma de México = National Autonomous University of Mexico [UNAM]
Pierce, Annick [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Perez-Cervera, Yobana [Auteur]
Universidad Nacional Autónoma de México = National Autonomous University of Mexico [UNAM]
Zenteno, Edgar [Auteur]
Universidad Nacional Autónoma de México = National Autonomous University of Mexico [UNAM]
Lefebvre, Tony [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Journal title :
Biochemical Society Transactions
Abbreviated title :
Biochem. Soc. Trans.
Volume number :
45
Pages :
365-370
Publication date :
2017-04-13
ISSN :
1470-8752
English keyword(s) :
Animals
O-GlcNAc transferase
Humans
beta-N-Acetylhexosaminidases
Acetylglucosamine
O-GlcNAcylation
Protein Processing, Post-Translational
N-Acetylglucosaminyltransferases
OGT
Acylation
O-GlcNAc transferase
Humans
beta-N-Acetylhexosaminidases
Acetylglucosamine
O-GlcNAcylation
Protein Processing, Post-Translational
N-Acetylglucosaminyltransferases
OGT
Acylation
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
O-GlcNAcylation is a highly dynamic post-translational modification whose level depends on nutrient status. Only two enzymes regulate O-GlcNAcylation cycling, the glycosyltransferase OGT (O-GlcNAc transferase) and the ...
Show more >O-GlcNAcylation is a highly dynamic post-translational modification whose level depends on nutrient status. Only two enzymes regulate O-GlcNAcylation cycling, the glycosyltransferase OGT (O-GlcNAc transferase) and the glycoside hydrolase OGA (O-GlcNAcase), that add and remove the GlcNAc moiety to and from acceptor proteins, respectively. During the last 30 years, OGT has emerged as a master regulator of cell life with O-GlcNAcylation being found in viruses, bacteria, insects, protists and metazoans. The study of OGT in different biological systems opens new perspectives for understanding this enzyme in many kingdoms of life. In this review, we summarize recent and older findings regarding the distribution of OGT in living organisms.Show less >
Show more >O-GlcNAcylation is a highly dynamic post-translational modification whose level depends on nutrient status. Only two enzymes regulate O-GlcNAcylation cycling, the glycosyltransferase OGT (O-GlcNAc transferase) and the glycoside hydrolase OGA (O-GlcNAcase), that add and remove the GlcNAc moiety to and from acceptor proteins, respectively. During the last 30 years, OGT has emerged as a master regulator of cell life with O-GlcNAcylation being found in viruses, bacteria, insects, protists and metazoans. The study of OGT in different biological systems opens new perspectives for understanding this enzyme in many kingdoms of life. In this review, we summarize recent and older findings regarding the distribution of OGT in living organisms.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
O-GlcNAcylation, signalisation cellulaire et cycle cellulaire
Submission date :
2020-02-12T15:11:51Z
2021-03-12T13:06:58Z
2021-03-12T13:06:58Z