Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes

被引:52
作者
Cosentino, Katia [1 ,2 ]
Ros, Uris [1 ,2 ,3 ]
Garcia-Saez, Ana J. [1 ,2 ]
机构
[1] Univ Tubingen, Interfac Inst Biochem IFIB, Tubingen, Germany
[2] Max Planck Inst Intelligent Syst, Stuttgart, Germany
[3] Univ Havana, Ctr Prot Studies, Havana, Cuba
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2016年 / 1858卷 / 03期
基金
欧洲研究理事会;
关键词
Pore forming proteins (PFPs); Pore forming toxins (PFTs); Protein oligomerization; Pore structure; Membrane; HEMOLYSIN-E HLYE; RAY CRYSTAL-STRUCTURE; COLICIN IA CHANNEL; EQUINATOXIN-II; ESCHERICHIA-COLI; X-RAY; PROAPOPTOTIC BAX; DIPHTHERIA-TOXIN; STRUCTURAL BASIS; STICHOLYSIN-II;
D O I
10.1016/j.bbamem.2015.09.013
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
Pore forming proteins (PFPs) share the ability of creating pores that allow the passage of ions, proteins or other constituents through a wide variety of target membranes, ranging from bacteria to humans. They often cause cell death, as pore formation disrupts the membrane permeability barrier required for maintaining cell homeostasis. The organization into supramolecular complexes or oligomers that pierce the membrane is a common feature of PFPs. However, the molecular pathway of self-assembly and pore opening remains unclear. Here, we review the most recent discoveries in the mechanism of membrane oligomerization and pore formation of a subset of PFPs, the alpha-PFPs, whose pore-forming domains are formed by helical segments. Only now we are starting to grasp the molecular details of their function, mainly thanks to the introduction of single molecule microscopy and nanoscopy techniques. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:457 / 466
页数:10
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