Titre :

Impact of proteotoxic stress on αB-crystallin partition, post-translational modifications, and interaction with desmin intermediate filaments protein

Auteur(s) :

Cieniewski, Caroline [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Claeyssen, charlotte [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Agbulut, Onnik [Auteur]
Bulangalire, Nathan [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]

Titre de la manifestation scientifique :

20èmes journées de la Société Française de Myologie

Ville :

La Baule

Pays :

France

Date de début de la manifestation scientifique :

2023-11-15

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

Myofibrillar myopathies are characterised by abnormal accumulation of misfolded myofibrillar proteins. In the case of desminopathies, desmin intermediate filaments aggregate taking away their partners, leading to a dramatic ...
Lire la suite >Myofibrillar myopathies are characterised by abnormal accumulation of misfolded myofibrillar proteins. In the case of desminopathies, desmin intermediate filaments aggregate taking away their partners, leading to a dramatic myofibrils disorganization and a loss of muscular function. The alphaB-crystallin (HSPB5), a small heat shock protein (sHSP), is a sensor for assembly of desmin intermediate filaments and a major chaperone in striated muscle cells. Over its chaperone activity, alphaB-crystallin is involved in several cellular functions such as cell integrity, cytoskeleton stabilization, or aggresome formation. The functions of alphaB-crystallin are modulated through post-translational modifications. Thus, alphaB-crystallin is known to be phosphorylated, phosphorylation interfering with its oligomerization and partition. Moreover, alphaB-crystallin is also modified by O-GlcNAcylation, an atypical glycosylation presenting a highly dynamic interplay with phosphorylation. Although little is known about alphaB-crystallin O-GlcNAcylation in muscle cells, recent reports demonstrated that O-GlcNAcylation could be involved in the modulation of its interaction with protein partners and in stress-induced translocation of alphaB-crystallin. Here we investigated in a cellular model of C2C12 myotubes how proteotoxic stress (i.e. proteasome inhibition) modifies the chaperone’s expression, its sub-cellular localization, and its interaction with desmin. We connected these results to the O-GlcNAcylation and the phosphorylation status of the sHSP. We expect to identify a post-translational modifications pattern on alphaB-crystallin that would maximize the chaperone benefits towards desmin aggregation.Lire moins >

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

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 :

2024-03-03T20:57:20Z
2024-03-06T08:38:12Z