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

Alexandre Pozza, François Giraud, Quentin Cece, Marina Casiraghi, Elodie Point, Marjorie Damian, Christel Le Bon, Karine Moncoq, Jean-Louis Banères, Ewen Lescop () and Laurent J. Catoire ()
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Alexandre Pozza: UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550)
François Giraud: Université Paris-Saclay
Quentin Cece: UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550)
Marina Casiraghi: UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550)
Elodie Point: UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550)
Marjorie Damian: Université de Montpellier, CNRS, ENSCM, Pôle Chimie Balard Recherche
Christel Le Bon: UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550)
Karine Moncoq: UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550)
Jean-Louis Banères: Université de Montpellier, CNRS, ENSCM, Pôle Chimie Balard Recherche
Ewen Lescop: Université Paris-Saclay
Laurent J. Catoire: UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550)

Nature Communications, 2022, vol. 13, issue 1, 1-16

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-29410-5

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