BAR Domain Scaffolds in Dynamin-Mediated Membrane Fission

被引：169
作者：
Daumke, Oliver [3 ,6 ]
Roux, Aurelien [4 ,5 ]
Haucke, Volker [1 ,2 ]
机构：
[1] Leibniz Inst Mol Pharmakol FMP, D-13125 Berlin, Germany
[2] Charite, D-10117 Berlin, Germany
[3] Max Delbruck Ctr Mol Med, D-13125 Berlin, Germany
[4] Univ Geneva, Dept Biochem, CH-1211 Geneva 4, Switzerland
[5] Swiss Natl Ctr Competence Res, Programme Chem Biol, CH-1211 Geneva, Switzerland
[6] Free Univ Berlin, Inst Chem & Biochem, D-14195 Berlin, Germany
来源：
CELL | 2014年 / 156卷 / 05期
基金：
瑞士国家科学基金会; 欧洲研究理事会;
关键词：
SYNAPTIC VESICLE ENDOCYTOSIS; CLATHRIN-COATED PITS; CRYSTAL-STRUCTURE; NERVE-TERMINALS; STRUCTURAL INSIGHTS; CONTAINING PROTEINS; SORTING NEXIN-9; SH3; DOMAIN; CURVATURE; ENDOPHILIN;
D O I：
10.1016/j.cell.2014.02.017
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：
Biological membranes undergo constant remodeling by membrane fission and fusion to change their shape and to exchange material between subcellular compartments. During clathrin-mediated endocytosis, the dynamic assembly and disassembly of protein scaffolds comprising members of the bin-amphiphysin-rvs (BAR) domain protein superfamily constrain the membrane into distinct shapes as the pathway progresses toward fission by the GTPase dynamin. In this Review, we discuss how BAR domain protein assembly and disassembly are controlled in space and time and which structural and biochemical features allow the tight regulation of their shape and function to enable dynamin-mediated membrane fission.
引用
收藏
页码：882 / 892
页数：11
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