Membrane pore formation at protein-lipid interfaces

被引:130
|
作者
Gilbert, Robert J. C. [1 ]
Serra, Mauro Dalla [2 ,3 ]
Froelich, Christopher J. [4 ,5 ]
Wallace, Mark I. [6 ]
Anderluh, Gregor [7 ,8 ]
机构
[1] Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Oxford OX3 7BN, England
[2] CNR, Ist Biofis, I-38123 Trento, Italy
[3] Fdn Bruno Kessler, I-38123 Trento, Italy
[4] NorthShore Univ Hlth Syst Res Inst, Evanston, IL 60201 USA
[5] Univ Chicago, Evanston, IL 60201 USA
[6] Univ Oxford, Dept Chem, Oxford OX1 3TA, England
[7] Univ Ljubljana, Biotech Fac, Dept Biol, Ljubljana 1000, Slovenia
[8] Natl Inst Chem, Ljubljana 1000, Slovenia
关键词
pore-forming peptides and proteins; toroidal pore formation; protein-membrane interactions; Bcl-2/colicin family proteins; actinoporins; MACPF/CDC family proteins; CHOLESTEROL-DEPENDENT CYTOLYSINS; HOST-CELL TRAVERSAL; BAX-DERIVED PEPTIDE; ALAMETHICIN PORE; DAMAGE MEMBRANES; STRUCTURAL BASIS; EQUINATOXIN-II; STICHOLYSIN-II; TOROIDAL PORE; LINE TENSION;
D O I
10.1016/j.tibs.2014.09.002
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) interact with lipid bilayers to compromise membrane integrity. Many PFPs function by inserting a ring of oligomerized subunits into the bilayer to form a protein-lined hydrophilic channel. However, mounting evidence suggests that PFPs can also generate 'proteolipidic' pores by contributing to the fusion of inner and outer bilayer leaflets to form a toroidal structure. We discuss here toroidal pore formation by peptides including melittin, protegrin, and Alzheimer's A beta 1-41, as well as by PFPs from several evolutionarily unrelated families: the colicin/Bcl-2 grouping including the pro-apoptotic protein Bax, actinoporins derived from sea anemones, and the membrane attack complex-perforin/cholesterol dependent cytolysin (MACPF/CDC) set of proteins. We also explore how the structure and biological role of toroidal pores might be investigated further.
引用
收藏
页码:510 / 516
页数:7
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