Amphipathic helices and membrane curvature

被引:417
作者
Drin, Guillaume [1 ]
Antonny, Bruno
机构
[1] Univ Nice Sophia Antipolis, F-06560 Valbonne, France
关键词
Membrane curvature; Amphipathic helix; Vesicular transport; Protein-lipid interaction; Lipid packing; N-BAR DOMAIN; ALPHA-SYNUCLEIN; PEPTIDE ANALOGS; COPII VESICLE; BINDING; THERMODYNAMICS; HELIX-0; ARFGAP1; LIPIDS; HYDROPHOBICITY;
D O I
10.1016/j.febslet.2009.10.022
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Numerous data have been collected on lipid-binding amphipathic helices involved in membrane-remodeling machineries and vesicular transport. Here we describe how, with regard to lipid composition, the physicochemical features of some amphipathic helices explain their ability to recognize membrane curvature or to participate in membrane remodeling. We propose that sensing highly-curved membranes requires that the polar and hydrophobic faces of the helix do not cooperate in lipid binding. A more detailed description of the interaction between amphipathic helices and lipids is however needed; notably to explain how new helices contribute to detection of modest changes in curvature or even negative curvature. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1840 / 1847
页数:8
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