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Updated: Feb 27, 2026

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
Published on: September 2, 2020
Membrane fluidity is a driving force for recoverin myristoyl immobilization in zwitterionic lipids
Kim Potvin-Fournier1, Geneviève Valois-Paillard1, Thierry Lefèvre2
1Département de Chimie, Regroupement Québécois de Recherche sur la Fonction, L'ingénierie et L'application des Protéines (PROTEO), Centre de Recherche sur les Matériaux Avancés (CERMA), Centre Québécois sur les Matériaux Fonctionnels (CQMF), Université Laval, Pavillon Alexandre-Vachon, 1045 Avenue de la Médecine, Québec, Québec G1V 0A6, Canada; CUO-Recherche, Centre de Recherche du CHU de Québec, Hôpital du Saint-Sacrement, Département d'ophtalmologie, Faculté de Médecine, PROTEO, Université Laval, Québec, Québec G1S 4L8, Canada.
Abstract:
Recoverin is the only protein for which the phenomenon of calcium-myristoyl switch has been demonstrated without ambiguity. It is located in rod disk membranes where the highest content in polyunsaturated lipid acyl chains can be found. However, although essential to better understand the inactivation of the phototransduction process, the role of membrane fluidity on recoverin recruitment is unclear. We have therefore investigated the immobilization of the recoverin myristoyl moiety in the presence of phosphocholine bilayers using 2H solid-state NMR spectroscopy. Several lipids with different acyl chains were selected to investigate model membranes characterized by different fluidity. Immobilization of the recoverin myristoyl moiety was successfully observed but only in the presence of calcium and in specific lipid disordered states, showing that an optimal fluidity is required for recoverin immobilization.
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