Contributors: Laboratoire de biologie physico-chimique des protéines membranaires (LBPC-PM (UMR_7099)); Institut de biologie physico-chimique (IBPC (FR_550)); Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité); Institut de Chimie des Substances Naturelles (ICSN); Institut de Chimie - CNRS Chimie (INC-CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS); Cibles Thérapeutiques et conception de médicaments (CiTCoM - UMR 8038); Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité); Department of Molecular and Cellular Physiology Stanford; Stanford Medicine; Stanford University-Stanford University; Institut des Biomolécules Max Mousseron Pôle Chimie Balard (IBMM); Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM); Université de Montpellier (UM); Centre National de la Recherche Scientifique (CNRS), Université de Paris and Université de Montpellier; A postdoctoral fellowship Marie Curie Global Fellowship for M.C. (AlloGPCR-799376); IR INFRANALYTICS FR2054 CNRS.; ANR-17-CE11-0011,allosig,allostérie, dynamique conformationnelle et signalisation via les RCPG(2017); ANR-11-LABX-0011,DYNAMO,Dynamique des membranes transductrices d'énergie : biogénèse et organisation supramoléculaire.(2011); ANR-11-EQPX-0008,CACSICE,Centre d'analyse de systèmes complexes dans les environnements complexes(2011)
نبذة مختصرة : International audience ; 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.
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