Titre :

O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle.

Auteur(s) :

Cieniewski-Bernard, Caroline [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Lambert, Matthias [Auteur]
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 - ULR 4488 [URePSSS]
Montel, Valérie [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
STEVENS, Laurence [Auteur]
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 - ULR 4488 [URePSSS]

Titre de la revue :

Frontiers in Physiology

Nom court de la revue :

Front Physiol

Numéro :

5

Pagination :

421

Date de publication :

2014-10-30

ISSN :

1664-042X

Mot(s)-clé(s) en anglais :

MLC2
O-GlcNAcylation
O-GlcNAcylation/phosphorylation interplay
contractile properties
contractile proteins
phosphorylation
sarcomeric structure

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

O-GlcNAcylation, a generally undermined atypical protein glycosylation process, is involved in a dynamic and highly regulated interplay with phosphorylation. Akin to phosphorylation, O-GlcNAcylation is also involved in the ...
Lire la suite >O-GlcNAcylation, a generally undermined atypical protein glycosylation process, is involved in a dynamic and highly regulated interplay with phosphorylation. Akin to phosphorylation, O-GlcNAcylation is also involved in the physiopathology of several acquired diseases, such as muscle insulin resistance or muscle atrophy. Recent data underline that the interplay between phosphorylation and O-GlcNAcylation acts as a modulator of skeletal muscle contractile activity. In particular, the O-GlcNAcylation level of the phosphoprotein myosin light chain 2 seems to be crucial in the modulation of the calcium activation properties, and should be responsible for changes in calcium properties observed in functional atrophy. Moreover, since several key structural proteins are O-GlcNAc-modified, and because of the localization of the enzymes involved in the O-GlcNAcylation/de-O-GlcNAcylation process to the nodal Z disk, a role of O-GlcNAcylation in the modulation of the sarcomeric structure should be considered.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Non spécifiée

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 :

2020-04-09T14:09:34Z
2020-04-10T08:39:23Z
2020-04-13T07:32:07Z