A new paradigm for membrane-organizing and -shaping scaffolds

被引:92
作者
Bauer, Manuel [1 ]
Pelkmans, Lucas [1 ]
机构
[1] Swiss Fed Inst Technol, ETH, Inst Mol Syst Biol, CH-8093 Zurich, Switzerland
来源
FEBS LETTERS | 2006年 / 580卷 / 23期
关键词
caveolin; reticulon; flotillin;
D O I
10.1016/j.febslet.2006.08.077
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
The clathrin, COPI and COPII scaffolds are paradigm vesicle coats in membrane trafficking. Recent advances in our understanding of the caveolar coat have generated a new paradigm. It represents those membrane coats, where a considerable part of the protein component is lipid modified, and integrated into the cytosolic leaflet of the vesicle membrane by a hairpin-like hydrophobic structure. Such coat proteins are permanently associated with membranes, and form oligomers early after synthesis. These oligomers assemble into a coat that has high affinity for particular lipids, creating lipid microdomains within the membrane. The combined protein-lipid structure should be considered as the scaffold that entraps ligands, either through affinity with the protein or with the lipid component, and that has the ability to shape membranes. Besides scaffolds assembled by cave-olins, scaffolds assembled by reticulons and PHB domain-containing proteins such as the reggielflotillin proteins fit this paradigm. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:5559 / 5564
页数:6
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