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Article Dans Une Revue Nature Communications Année : 2022

Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure

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Alexandre Pozza
  • Fonction : Auteur
François Giraud
  • Fonction : Auteur
Quentin Cece
  • Fonction : Auteur
Marina Casiraghi
  • Fonction : Auteur
Elodie Point
  • Fonction : Auteur
Marjorie Damian
  • Fonction : Auteur
Christel Le Bon
Karine Moncoq
  • Fonction : Auteur
Jean-Louis Banères
Ewen Lescop
Laurent Catoire

Résumé

Abstract Cell membranes represent a complex and variable medium in time and space of lipids and proteins. Their physico-chemical properties are determined by lipid components which can in turn influence the biological function of membranes. Here, we used hydrostatic pressure to study the close dynamic relationships between lipids and membrane proteins. Experiments on the β –barrel OmpX and the α –helical BLT2 G Protein-Coupled Receptor in nanodiscs of different lipid compositions reveal conformational landscapes intimately linked to pressure and lipids. Pressure can modify the conformational landscape of the membrane protein per se, but also increases the gelation of lipids, both being monitored simultaneously at high atomic resolution by NMR. Our study also clearly shows that a membrane protein can modulate, at least locally, the fluidity of the bilayer. The strategy proposed herein opens new perspectives to scrutinize the dynamic interplay between membrane proteins and their surrounding lipids.

Domaines

Biophysique

Dates et versions

hal-03852463 , version 1 (15-11-2022)

Identifiants

Citer

Alexandre Pozza, François Giraud, Quentin Cece, Marina Casiraghi, Elodie Point, et al.. Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure. Nature Communications, 2022, 13 (1), pp.1780. ⟨10.1038/s41467-022-29410-5⟩. ⟨hal-03852463⟩
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