Cyclin D1 Stability Is Partly Controlled ...
Document type :
Article dans une revue scientifique
DOI :
Permalink :
Title :
Cyclin D1 Stability Is Partly Controlled by O-GlcNAcylation
Author(s) :
Masclef, Louis [Auteur]
Dehennaut, Vanessa [Auteur]
Mécanismes de la Tumorigénèse et Thérapies Ciblées (M3T) - UMR 8161
Mécanismes de la Tumorigénèse et Thérapies Ciblées - UMR 8161 [M3T]
mortuaire, marlène [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Schulz, Celine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Leturcq, Maïté [Auteur]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Edouart (vercoutter), Anne-Sophie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Dehennaut, Vanessa [Auteur]

Mécanismes de la Tumorigénèse et Thérapies Ciblées (M3T) - UMR 8161
Mécanismes de la Tumorigénèse et Thérapies Ciblées - UMR 8161 [M3T]
mortuaire, marlène [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Schulz, Celine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Leturcq, Maïté [Auteur]
Lefebvre, Tony [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Edouart (vercoutter), Anne-Sophie [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Journal title :
Frontiers in Endocrinology
Abbreviated title :
Front. Endocrinol.
Volume number :
10
Publisher :
Frontiers Media SA
Publication date :
2019-02-22
ISSN :
1664-2392
English keyword(s) :
cyclin D
O-GlcNAc
stability
ubiquitination
cell cycle
O-GlcNAc
stability
ubiquitination
cell cycle
HAL domain(s) :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Cyclin D1 is the regulatory partner of the cyclin-dependentkinases (CDKs) CDK4 orCDK6. Once associated and activated, the cyclin D1/CDK complexes drive the cellcycle entry and G1 phase progression in response to extracellular ...
Show more >Cyclin D1 is the regulatory partner of the cyclin-dependentkinases (CDKs) CDK4 orCDK6. Once associated and activated, the cyclin D1/CDK complexes drive the cellcycle entry and G1 phase progression in response to extracellular signals. To ensure theirtimely and accurate activation during cell cycle progression, cyclin D1 turnover is finelycontrolled by phosphorylation and ubiquitination. Here weshow that the dynamic andreversibleO-linkedβ-N-Acetyl-glucosaminylation (O-GlcNAcylation) regulates also cyclinD1 half-life. HighO-GlcNAc levels increase the stability of cyclin D1, while reduction ofO-GlcNAcylation strongly decreases it. Moreover, elevation ofO-GlcNAc levels throughO-GlcNAcase (OGA) inhibition significantly slows down the ubiquitination of cyclin D1.Finally, biochemical and cell imaging experiments in humancancer cells reveal that theO-GlcNAc transferase (OGT) binds to and glycosylates cyclinD1. We conclude thatO-GlcNAcylation promotes the stability of cyclin D1 throughmodulating its ubiquitination.Show less >
Show more >Cyclin D1 is the regulatory partner of the cyclin-dependentkinases (CDKs) CDK4 orCDK6. Once associated and activated, the cyclin D1/CDK complexes drive the cellcycle entry and G1 phase progression in response to extracellular signals. To ensure theirtimely and accurate activation during cell cycle progression, cyclin D1 turnover is finelycontrolled by phosphorylation and ubiquitination. Here weshow that the dynamic andreversibleO-linkedβ-N-Acetyl-glucosaminylation (O-GlcNAcylation) regulates also cyclinD1 half-life. HighO-GlcNAc levels increase the stability of cyclin D1, while reduction ofO-GlcNAcylation strongly decreases it. Moreover, elevation ofO-GlcNAc levels throughO-GlcNAcase (OGA) inhibition significantly slows down the ubiquitination of cyclin D1.Finally, biochemical and cell imaging experiments in humancancer cells reveal that theO-GlcNAc transferase (OGT) binds to and glycosylates cyclinD1. We conclude thatO-GlcNAcylation promotes the stability of cyclin D1 throughmodulating its ubiquitination.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
O-GlcNAcylation, signalisation cellulaire et cycle cellulaire
Submission date :
2020-12-07T10:32:50Z
2020-12-07T17:58:14Z
2020-12-07T17:58:14Z
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