Mapping of O-linked beta-N-acetylglucosamine ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Mapping of O-linked beta-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle.
Auteur(s) :
Hédou, Julie [Auteur]
Université de Lille
Bastide, Bruno [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Page, Adeline [Auteur]
Université de Lille
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Morelle, Willy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Université de Lille
Bastide, Bruno [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Page, Adeline [Auteur]
Université de Lille
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Morelle, Willy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Titre de la revue :
Proteomics
Nom court de la revue :
Proteomics
Numéro :
9
Pagination :
2139-48
Date de publication :
2009-04-01
ISSN :
1615-9861
Mot(s)-clé(s) en anglais :
Acetylglucosamine
Actins
Animals
Glycosylation
Muscle Proteins
Muscle
Skeletal
Myosin Heavy Chains
Myosin Light Chains
Peptide Mapping
Protein Processing
Post-Translational
Rats
Serine
Tandem Mass Spectrometry
Actins
Animals
Glycosylation
Muscle Proteins
Muscle
Skeletal
Myosin Heavy Chains
Myosin Light Chains
Peptide Mapping
Protein Processing
Post-Translational
Rats
Serine
Tandem Mass Spectrometry
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
O-linked beta-N-acetylglucosamine (O-GlcNAc) is a widespread modification of serine/threonine residues of nucleocytoplasmic proteins. Recently, several key contractile proteins in rat skeletal muscle (i.e., myosin heavy ...
Lire la suite >O-linked beta-N-acetylglucosamine (O-GlcNAc) is a widespread modification of serine/threonine residues of nucleocytoplasmic proteins. Recently, several key contractile proteins in rat skeletal muscle (i.e., myosin heavy and light chains and actin) were identified as O-GlcNAc modified. Moreover, it was demonstrated that O-GlcNAc moieties involved in contractile protein interactions could modulate Ca(2+) activation parameters of contraction. In order to better understand how O-GlcNAc can modulate the contractile activity of muscle fibers, we decided to identify the sites of O-GlcNAc modification in purified contractile protein homogenates. Using an MS-based method that relies on mild beta-elimination followed by Michael addition of DTT (BEMAD), we determined the localization of one O-GlcNAc site in the subdomain four of actin and four O-GlcNAc sites in the light meromyosin region of myosin heavy chains (MHC). According to previous reports concerning the role of these regions, our data suggest that O-GlcNAc sites might modulate the actin-tropomyosin interaction, and be involved in MHC polymerization or interactions between MHC and other contractile proteins. Thus, the results suggest that this PTM might be involved in protein-protein interactions but could also modulate the contractile properties of skeletal muscle.Lire moins >
Lire la suite >O-linked beta-N-acetylglucosamine (O-GlcNAc) is a widespread modification of serine/threonine residues of nucleocytoplasmic proteins. Recently, several key contractile proteins in rat skeletal muscle (i.e., myosin heavy and light chains and actin) were identified as O-GlcNAc modified. Moreover, it was demonstrated that O-GlcNAc moieties involved in contractile protein interactions could modulate Ca(2+) activation parameters of contraction. In order to better understand how O-GlcNAc can modulate the contractile activity of muscle fibers, we decided to identify the sites of O-GlcNAc modification in purified contractile protein homogenates. Using an MS-based method that relies on mild beta-elimination followed by Michael addition of DTT (BEMAD), we determined the localization of one O-GlcNAc site in the subdomain four of actin and four O-GlcNAc sites in the light meromyosin region of myosin heavy chains (MHC). According to previous reports concerning the role of these regions, our data suggest that O-GlcNAc sites might modulate the actin-tropomyosin interaction, and be involved in MHC polymerization or interactions between MHC and other contractile proteins. Thus, the results suggest that this PTM might be involved in protein-protein interactions but could also modulate the contractile properties of skeletal muscle.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
Université de Lille
Univ. Artois
Univ. Littoral Côte d’Opale
Univ. Artois
Univ. Littoral Côte d’Opale
Équipe(s) de recherche :
Activité Physique, Muscle, Santé (APMS)
Date de dépôt :
2020-07-20T15:28:25Z
2020-08-18T12:02:44Z
2020-08-18T12:02:44Z
Fichiers
- Hedou et alM606787.pdf
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