Titre :

Global O-GlcNAcylation changes impact desmin phosphorylation and its partition toward cytoskeleton in C2C12 skeletal muscle cells differentiated into myotubes.

Auteur(s) :

Claeyssen, Charlotte [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Bastide, Bruno [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Cieniewski, Caroline [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369

Titre de la revue :

Scientific Reports

Nom court de la revue :

Sci Rep

Numéro :

12

Pagination :

9831

Date de publication :

2022-06-14

ISSN :

2045-2322

Mot(s)-clé(s) en anglais :

Acetylglucosamine
Cytoskeleton
Desmin
Muscle Fibers, Skeletal
Muscle, Skeletal
Phosphorylation
Protein Processing, Post-Translational

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

Desmin is the guardian of striated muscle integrity, permitting the maintenance of muscle shape and the efficiency of contractile activity. It is also a key mediator of cell homeostasis and survival. To ensure the fine ...
Lire la suite >Desmin is the guardian of striated muscle integrity, permitting the maintenance of muscle shape and the efficiency of contractile activity. It is also a key mediator of cell homeostasis and survival. To ensure the fine regulation of skeletal muscle processes, desmin is regulated by post-translational modifications (PTMs). It is more precisely phosphorylated by several kinases connecting desmin to intracellular processes. Desmin is also modified by O-GlcNAcylation, an atypical glycosylation. However, the functional consequence of O-GlcNAcylation on desmin is still unknown, nor its impact on desmin phosphorylation. In a model of C2C12 myotubes, we modulated the global O-GlcNAcylation level, and we determined whether the expression, the PTMs and the partition of desmin toward insoluble material or cytoskeleton were impacted or not. We have demonstrated in the herein paper that O-GlcNAcylation variations led to changes in desmin behaviour. In particular, our data clearly showed that O-GlcNAcylation increase led to a decrease of phosphorylation level on desmin that seems to involve CamKII correlated to a decrease of its partition toward cytoskeleton. Our data showed that phosphorylation/O-GlcNAcylation interplay is highly complex on desmin, supporting that a PTMs signature could occur on desmin to finely regulate its partition (i.e. distribution) with a spatio-temporal regulation.Lire moins >

Comité de lecture :

Oui

Audience :

Internationale

Établissement(s) :

Université de Lille
Univ. Artois
Univ. Littoral Côte d’Opale

Collections :

• Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369

Équipe(s) de recherche :

Activité Physique, Muscle, Santé (APMS)

Date de dépôt :

2022-07-05T07:55:40Z
2022-07-06T06:58:53Z