Detection and identification of O-GlcNAcylated ...
Document type :
Article dans une revue scientifique
DOI :
PMID :
Permalink :
Title :
Detection and identification of O-GlcNAcylated proteins by proteomic approaches
Author(s) :
Edouart (vercoutter), Anne-Sophie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Belkoura, Ikram [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Guinez, Celine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Baldini, Steffi F. [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Leturcq, Maïté [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
mortuaire, marlène [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Mir, Anne-Marie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Steenackers, Agata [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Dehennaut, Vanessa [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Pierce, Annick [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Belkoura, Ikram [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Guinez, Celine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Baldini, Steffi F. [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Leturcq, Maïté [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
mortuaire, marlène [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Mir, Anne-Marie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Steenackers, Agata [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Dehennaut, Vanessa [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Pierce, Annick [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Journal title :
Proteomics
Abbreviated title :
Proteomics
Volume number :
15
Pages :
1039-1050
Publication date :
2015-03
ISSN :
1615-9861
English keyword(s) :
Post-translational modification
Cell Line
Humans
Glycoprotein
Rats
Acetylglucosamine
Glycosylation
Site mapping
O-GlcNAcome
Tandem Mass Spectrometry
Glycoproteomics
Animals
Mass Spectrometry
Proteomics
O-GlcNAcylation
Mice
Protein Processing, Post-Translational
Cell Line
Humans
Glycoprotein
Rats
Acetylglucosamine
Glycosylation
Site mapping
O-GlcNAcome
Tandem Mass Spectrometry
Glycoproteomics
Animals
Mass Spectrometry
Proteomics
O-GlcNAcylation
Mice
Protein Processing, Post-Translational
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
O-GlcNAcylation (O-linked beta-N-acetylglucosaminylation) is a widespread PTM confined within the nuclear, the cytosolic, and the mitochondrial compartments of eukaryotes. Recently, O-GlcNAcylation has been also detected ...
Show more >O-GlcNAcylation (O-linked beta-N-acetylglucosaminylation) is a widespread PTM confined within the nuclear, the cytosolic, and the mitochondrial compartments of eukaryotes. Recently, O-GlcNAcylation has been also detected in the close vicinity of plasma membranes particularly in lipid microdomains. The detection of this PTM can be easily done if appropriate controls and precautions are taken using a wide variety of tools including lectins, antibodies, or click-chemistry-based methods. In contrast, the identification of the proteins bearing O-GlcNAc moieties and the localization of the precise sites of O-GlcNAcylation remain challenging. This is due to the lability of the glycosidic bond between hydroxyl group of serine or threonine and N-acetylglucosamine using conventional fragmentation techniques such as CID. To tentatively overcome this technical limitation, electron-capture dissociation, or electron-transfer dissociation MS/MS are now used. Thanks to these breakthroughs, a large number of O-GlcNAc sites have been identified to date but these methodologies remain far from being used in routine.Show less >
Show more >O-GlcNAcylation (O-linked beta-N-acetylglucosaminylation) is a widespread PTM confined within the nuclear, the cytosolic, and the mitochondrial compartments of eukaryotes. Recently, O-GlcNAcylation has been also detected in the close vicinity of plasma membranes particularly in lipid microdomains. The detection of this PTM can be easily done if appropriate controls and precautions are taken using a wide variety of tools including lectins, antibodies, or click-chemistry-based methods. In contrast, the identification of the proteins bearing O-GlcNAc moieties and the localization of the precise sites of O-GlcNAcylation remain challenging. This is due to the lability of the glycosidic bond between hydroxyl group of serine or threonine and N-acetylglucosamine using conventional fragmentation techniques such as CID. To tentatively overcome this technical limitation, electron-capture dissociation, or electron-transfer dissociation MS/MS are now used. Thanks to these breakthroughs, a large number of O-GlcNAc sites have been identified to date but these methodologies remain far from being used in routine.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Research team(s) :
O-GlcNAcylation, signalisation cellulaire et cycle cellulaire
Submission date :
2020-02-12T15:11:52Z
2021-03-18T12:16:27Z
2021-03-18T12:16:27Z