O-GlcNAcylation is a key modulator of ...
Document type :
Article dans une revue scientifique
PMID :
Permalink :
Title :
O-GlcNAcylation is a key modulator of skeletal muscle sarcomeric morphometry associated to modulation of protein-protein interactions
Author(s) :
Lambert, Matthias [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Richard, Elodie [Auteur]
Duban-Deweer, Sophie [Auteur]
Krzewinski, Frederic [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Deracinois, Barbara [Auteur]
BioEcoAgro - UMR-T 1158
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Dupont, Erwan [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Bastide, Bruno [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Cieniewski, Caroline [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Richard, Elodie [Auteur]
Duban-Deweer, Sophie [Auteur]
Krzewinski, Frederic [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Deracinois, Barbara [Auteur]

BioEcoAgro - UMR-T 1158
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Dupont, Erwan [Auteur]

Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Bastide, Bruno [Auteur]

Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Cieniewski, Caroline [Auteur]

Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Journal title :
Biochimica et biophysica acta. General subjects
Abbreviated title :
Biochim. Biophys. Acta-Gen. Subj.
Volume number :
1860
Pages :
2017-2030
Publication date :
2016-09-01
ISSN :
0304-4165
English keyword(s) :
Cell Line
Muscle Fibers
Skeletal
Muscle
Skeletal
Myofibrils
Protein Interaction Maps
Protein Processing
Post-Translational
Proteome
Sarcomeres
Desmin
O-GlcNAcylation
Protein–protein interactions
Sarcomere structure
Skeletal muscle cells
αB-crystallin
Muscle Fibers
Skeletal
Muscle
Skeletal
Myofibrils
Protein Interaction Maps
Protein Processing
Post-Translational
Proteome
Sarcomeres
Desmin
O-GlcNAcylation
Protein–protein interactions
Sarcomere structure
Skeletal muscle cells
αB-crystallin
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
The sarcomere structure of skeletal muscle is determined through multiple protein-protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this ...
Show more >The sarcomere structure of skeletal muscle is determined through multiple protein-protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylation, a post-translational modification modifying several key structural proteins and previously described as a modulator of the contractile activity, was never considered to date in the sarcomeric organization. C2C12 skeletal myotubes were treated with Thiamet-G (OGA inhibitor) in order to increase the global O-GlcNAcylation level. Our data clearly showed a modulation of the O-GlcNAc level more sensitive and dynamic in the myofilament-enriched fraction than total proteome. This fine O-GlcNAc level modulation was closely related to changes of the sarcomeric morphometry. Indeed, the dark-band and M-line widths increased, while the I-band width and the sarcomere length decreased according to the myofilament O-GlcNAc level. Some structural proteins of the sarcomere such as desmin, αB-crystallin, α-actinin, moesin and filamin-C have been identified within modulated protein complexes through O-GlcNAc level variations. Their interactions seemed to be changed, especially for desmin and αB-crystallin. For the first time, our findings clearly demonstrate that O-GlcNAcylation, through dynamic regulations of the structural interactome, could be an important modulator of the sarcomeric structure and may provide new insights in the understanding of molecular mechanisms of neuromuscular diseases characterized by a disorganization of the sarcomeric structure. In the present study, we demonstrated a role of O-GlcNAcylation in the sarcomeric structure modulation.Show less >
Show more >The sarcomere structure of skeletal muscle is determined through multiple protein-protein interactions within an intricate sarcomeric cytoskeleton network. The molecular mechanisms involved in the regulation of this sarcomeric organization, essential to muscle function, remain unclear. O-GlcNAcylation, a post-translational modification modifying several key structural proteins and previously described as a modulator of the contractile activity, was never considered to date in the sarcomeric organization. C2C12 skeletal myotubes were treated with Thiamet-G (OGA inhibitor) in order to increase the global O-GlcNAcylation level. Our data clearly showed a modulation of the O-GlcNAc level more sensitive and dynamic in the myofilament-enriched fraction than total proteome. This fine O-GlcNAc level modulation was closely related to changes of the sarcomeric morphometry. Indeed, the dark-band and M-line widths increased, while the I-band width and the sarcomere length decreased according to the myofilament O-GlcNAc level. Some structural proteins of the sarcomere such as desmin, αB-crystallin, α-actinin, moesin and filamin-C have been identified within modulated protein complexes through O-GlcNAc level variations. Their interactions seemed to be changed, especially for desmin and αB-crystallin. For the first time, our findings clearly demonstrate that O-GlcNAcylation, through dynamic regulations of the structural interactome, could be an important modulator of the sarcomeric structure and may provide new insights in the understanding of molecular mechanisms of neuromuscular diseases characterized by a disorganization of the sarcomeric structure. In the present study, we demonstrated a role of O-GlcNAcylation in the sarcomeric structure modulation.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
INRA
ISA
Univ. Artois
Univ. Littoral Côte d’Opale
Université de Lille
ISA
Univ. Artois
Univ. Littoral Côte d’Opale
Université de Lille
Collections :
Research team(s) :
Activité Physique, Muscle, Santé (APMS)
Submission date :
2019-09-24T10:01:15Z
2019-11-22T10:35:22Z
2020-05-13T14:25:17Z
2020-11-12T14:26:25Z
2019-11-22T10:35:22Z
2020-05-13T14:25:17Z
2020-11-12T14:26:25Z
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