Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
01 04 2022
01 04 2022
Historique:
received:
22
03
2021
accepted:
14
03
2022
entrez:
2
4
2022
pubmed:
3
4
2022
medline:
6
4
2022
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 35365643
doi: 10.1038/s41467-022-29410-5
pii: 10.1038/s41467-022-29410-5
pmc: PMC8975810
doi:
Substances chimiques
Lipid Bilayers
0
Membrane Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1780Informations de copyright
© 2022. The Author(s).
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