O-GlcNAcylation links ChREBP and FXR to ...
Type de document :
Compte-rendu et recension critique d'ouvrage
DOI :
PMID :
Titre :
O-GlcNAcylation links ChREBP and FXR to glucose-sensing
Auteur(s) :
Benhamed, Fadila [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Filhoulaud, Gaelle [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Caron, Sandrine [Auteur]
Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD]
Lefebvre, Philippe [Auteur]
Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD]
Staels, Bart [Auteur]
Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD]
Postic, Catherine [Auteur correspondant]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Filhoulaud, Gaelle [Auteur]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Caron, Sandrine [Auteur]
Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD]
Lefebvre, Philippe [Auteur]
Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD]
Staels, Bart [Auteur]
Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD]
Postic, Catherine [Auteur correspondant]
Institut Cochin [IC UM3 (UMR 8104 / U1016)]
Titre de la revue :
Frontiers in Endocrinology
Pagination :
230
Éditeur :
Frontiers
Date de publication :
2015-01-13
ISSN :
1664-2392
Mot(s)-clé(s) en anglais :
liver metabolism
ChREBP
glucose-sensing
O-GlcNAcylation
FXR
ChREBP
glucose-sensing
O-GlcNAcylation
FXR
Discipline(s) HAL :
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
Résumé en anglais : [en]
Accumulating evidence suggests that O-GlcNAc transferase, an enzyme responsible for O-GlcNAc post-translational modification acts as a nutrient sensor that links glucose and the hexosamine biosynthetic pathway to the ...
Lire la suite >Accumulating evidence suggests that O-GlcNAc transferase, an enzyme responsible for O-GlcNAc post-translational modification acts as a nutrient sensor that links glucose and the hexosamine biosynthetic pathway to the regulation of transcriptional factors involved in energy homeostasis. In liver, glucose signaling is mediated by carbohydrate response element-binding protein (ChREBP), which stimulates glycolytic and lipogenic gene expres-sion through its binding on a specific ChoRE DNA sequence. Modulation of ChREBP by O-GlcNAcylation increases its DNA binding affinity and its activity. ChREBP transcriptional activity also depends on the presence of several other co-factors and transcriptional fac-tors. Among them, the nuclear Farnesoid X Receptor (FXR), a key transcription factor of bile acid metabolism involved in the gut–liver axis homeostasis was recently shown to directly interact with ChREBP, acting as a repressor on the ChoRE of glycolytic genes. Interestingly, similarly to ChREBP, FXR is O-GlcNAcylated in response to glucose. This review discusses the importance of ChREBP and FXR modifications through O-GlcNAcylation in liver and how glucose can modify their mutual affinity and transcriptional activity.Lire moins >
Lire la suite >Accumulating evidence suggests that O-GlcNAc transferase, an enzyme responsible for O-GlcNAc post-translational modification acts as a nutrient sensor that links glucose and the hexosamine biosynthetic pathway to the regulation of transcriptional factors involved in energy homeostasis. In liver, glucose signaling is mediated by carbohydrate response element-binding protein (ChREBP), which stimulates glycolytic and lipogenic gene expres-sion through its binding on a specific ChoRE DNA sequence. Modulation of ChREBP by O-GlcNAcylation increases its DNA binding affinity and its activity. ChREBP transcriptional activity also depends on the presence of several other co-factors and transcriptional fac-tors. Among them, the nuclear Farnesoid X Receptor (FXR), a key transcription factor of bile acid metabolism involved in the gut–liver axis homeostasis was recently shown to directly interact with ChREBP, acting as a repressor on the ChoRE of glycolytic genes. Interestingly, similarly to ChREBP, FXR is O-GlcNAcylated in response to glucose. This review discusses the importance of ChREBP and FXR modifications through O-GlcNAcylation in liver and how glucose can modify their mutual affinity and transcriptional activity.Lire moins >
Langue :
Anglais
Vulgarisation :
Non
Projet ANR :
Commentaire :
Mini review article
Source :
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