Impact of proteotoxic stress on αB-crystallin partition, post-translational modifications, and interaction with desmin intermediate filaments protein - Université de Lille
Poster De Conférence Année : 2023

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

Résumé

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.
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Dates et versions

hal-04491555 , version 1 (06-03-2024)

Identifiants

  • HAL Id : hal-04491555 , version 1

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Caroline Cieniewski, Charlotte Claeyssen, Onnik Agbulut, Nathan Bulangalire. Impact of proteotoxic stress on αB-crystallin partition, post-translational modifications, and interaction with desmin intermediate filaments protein. 20èmes journées de la Société Française de Myologie, Nov 2023, La Baule, France. ⟨hal-04491555⟩
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