Modulation of the interaction and organization of Human Dystrophin repeats 11-15 subdomain with Membrane - Archive ouverte HAL Accéder directement au contenu
Poster De Conférence Année : 2011

Modulation of the interaction and organization of Human Dystrophin repeats 11-15 subdomain with Membrane

Résumé

Dystrophin is essential to skeletal muscle function and confers resistance to the sarcolemma by interacting with cytoskeleton and membrane. In the present work, we characterized the behavior of dystrophin 11–15 (DYS R11–15), five spectrin-like repeats from the central domain of human dystrophin, with lipids. DYS R11–15 displays an amphiphilic character at the liquid/air interface while maintaining its secondary α-helical structure. The interaction of DYS R11–15 with small unilamellar vesicles (SUVs) depends on the lipid nature, which is not the case with large unilamellar vesicles (LUVs). In addition, switching from anionic SUVs to anionic LUVs suggests the lipid packing as a crucial factor for the interaction of protein and lipid. The monolayer model and the modulation of surface pressure aim to mimic the muscle at work (i.e. dynamic changes of muscle membrane during contraction and relaxation) (high and low surface pressure). Strikingly, the lateral pressure modifies the protein organization. Increasing the lateral pressure leads the proteins to be organized in a regular network. Nevertheless, a different protein conformation after its binding to monolayer is revealed by trypsin proteolysis. Label-free quantification by nano-LC/MS/MS allowed identification of the helices in repeats 12 and 13 involved in the interaction with anionic SUVs. These results, combined with our previous studies, indicate that DYS R11–15 constitutes the only part of dystrophin that interacts with anionic as well as zwitterionic lipids and adapts its interaction and organization depending on lipid packing and lipid nature. We provide strong experimental evidence for a physiological role of the central domain of dystrophin in sarcolemma scaffolding through modulation of lipid-protein interactions.
Fichier non déposé

Dates et versions

hal-01454401 , version 1 (02-02-2017)

Identifiants

  • HAL Id : hal-01454401 , version 1
  • PRODINRA : 215935
  • WOS : 000293637300077

Citer

Joe Sarkis, Jean François Hubert,, Baptiste Legrand, Estelle Robert, Angélique Cheron, et al.. Modulation of the interaction and organization of Human Dystrophin repeats 11-15 subdomain with Membrane. 8th EBSA European Biophysics Congress, Aug 2011, Budapest, Hungary. , European Biophysics Journal, 40 issue 1, 2011, European Biophysics Journal. ⟨hal-01454401⟩
258 Consultations
0 Téléchargements

Partager

Gmail Facebook X LinkedIn More