Membrane fluidity is a driving force for recoverin myristoyl immobilization in zwitterionic lipids.

Kim Potvin-Fournier, Geneviève Valois-Paillard, Thierry Lefèvre, Line Cantin, Christian Salesse, Michèle Auger

Biochemical and biophysical research communications 2017 Sep 02

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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. Copyright © 2017 Elsevier Inc. All rights reserved.

Citation

Kim Potvin-Fournier, Geneviève Valois-Paillard, Thierry Lefèvre, Line Cantin, Christian Salesse, Michèle Auger. Membrane fluidity is a driving force for recoverin myristoyl immobilization in zwitterionic lipids. Biochemical and biophysical research communications. 2017 Sep 02;490(4):1268-1273