Mechanisms of Membrane Curvature Sensing

被引:326
|
作者
Antonny, Bruno [1 ,2 ]
机构
[1] Univ Nice Sophia Antipolis, F-06560 Valbonne, France
[2] CNRS, Inst Pharmacol Mol & Cellulaire, F-06560 Valbonne, France
来源
关键词
alpha-synuclein; ALPS motif; amphipathic helix; BAR domain; lipid packing; membrane electrostatics; OXYSTEROL-BINDING-PROTEIN; CTP-PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE; GTPASE-ACTIVATING-PROTEIN; ALPHA-SYNUCLEIN; GOLGI-APPARATUS; TRANS-GOLGI; AMPHIPATHIC HELICES; PLASMA-MEMBRANE; LIPID-MEMBRANES; COPI VESICLES;
D O I
10.1146/annurev-biochem-052809-155121
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
Bacteria and eukaryotic cells contain geometry-sensing tools in their cytosol: protein motifs or domains that recognize the curvature, concave or convex, deep or shallow, of lipid membranes. These sensors contrast with classical lipid-binding domains by their extended structure and, sometimes, counterintuitive chemistry. Among the sensors are long amphipathic helices, such as the ALPS motif and the N-terminal region of alpha-synuclein, whose apparent "design defects" translate into a remarkable ability to specifically adsorb to the surface of small vesicles. Fundamental differences in the lipid composition of membranes of the early and late secretory pathways probably explain why some sensors use mostly electrostatics whereas others take advantage of the hydrophobic effect. Membrane curvature sensors help to organize very diverse reactions, such as lipid transfer between membranes, the tethering of vesicles at the Golgi apparatus, and the assembly-disassembly cycle of protein coats.
引用
收藏
页码:101 / 123
页数:23
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