Journal Article

A sub-nanometre view of how membrane curvature and composition modulate lipid packing and protein recruitment

Vanni, Stefano, Gautier, Romain, Barelli, Hélène, Hirose, Hisaaki, Antonny, Bruno

2014

Overview

Two parameters of biological membranes, curvature and lipid composition, direct the recruitment of many peripheral proteins to cellular organelles. Although these traits are often studied independently, it is their combination that generates the unique interfacial properties of cellular membranes. Here, we use a combination of in vivo , in vitro and in silico approaches to provide a comprehensive map of how these parameters modulate membrane adhesive properties. The correlation between the membrane partitioning of model amphipathic helices and the distribution of lipid-packing defects in membranes of different shape and composition explains how macroscopic membrane properties modulate protein recruitment by changing the molecular topography of the membrane interfacial region. Furthermore, our results suggest that the range of conditions that can be obtained in a cellular context is remarkably large because lipid composition and curvature have, under most circumstances, cumulative effects. Membrane curvature and lipid composition direct the binding of many peripheral membrane proteins. Here, Vanni et al. use a combination of in vitro and molecular dynamics approaches to quantify how lipid-packing defects in membranes of various composition and curvature dictate the membrane adsorption of a model lipid-binding protein.

• Publisher: Nature Publishing Group UK,Nature Publishing Group
• Subject: 119/118 / 14/35 / 631/45/287/1192 / 631/45/612/1237 / 631/57/2271 / 631/80/313/2375 / 9/10 / Biological membranes / Cell Adhesion / Cell Line, Transformed / Cell Membrane - chemistry / Cell Membrane - metabolism / Cell Membrane - ultrastructure / Cell Shape / Dimyristoylphosphatidylcholine - chemistry / Epithelial Cells - metabolism / Epithelial Cells - ultrastructure / Fatty Acids - chemistry / Gene Expression / Green Fluorescent Proteins - chemistry / Green Fluorescent Proteins - genetics / Green Fluorescent Proteins - metabolism / GTPase-Activating Proteins - chemistry / GTPase-Activating Proteins - genetics / GTPase-Activating Proteins - metabolism / Humanities and Social Sciences / Humans / Hydrophobic and Hydrophilic Interactions / Lipid Bilayers - chemistry / Lipid Bilayers - metabolism / Molecular Dynamics Simulation / multidisciplinary / Phosphatidylcholines - chemistry / Recombinant Fusion Proteins - chemistry / Recombinant Fusion Proteins - genetics / Recombinant Fusion Proteins - metabolism / Retinal Pigment Epithelium - metabolism / Retinal Pigment Epithelium - ultrastructure / Science / Science (multidisciplinary)