Protein-lipid interactions and non-lamellar lipidic structures in membrane pore formation and membrane fusion
Protein-lipid interactions and non-lamellar lipidic structures in membrane pore formation and membrane fusion
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DOI：
10.1016/j.bbamem.2015.11.026
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发表时间：
2016-03-01
影响因子：
3.4
通讯作者：
Gilbert, Robert J. C.
中科院分区：
文献类型：
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作者：
Gilbert, Robert J. C.
成孔蛋白和多肽作用于它们的目标脂质双分子层膜以增加通透性。这种调节生物功能的方法与许多生命过程有关，包括；感染、寄生、免疫、细胞凋亡、发育和神经退行性变。虽然一些成孔蛋白/多肽组装成亚基环，以产生离散的、明确的成孔结构，但越来越多的成孔蛋白/多肽被认为是通过协同膜脂自身的机制形成孔的。其中，膜攻击复合物-穿孔素/胆固醇依赖性细胞溶血素（MACPF/CDC）家族蛋白、Bax/colidn家族蛋白和放射线机会蛋白尤为突出，其作用机制包括非层状（半环状或环状）脂质结构的形成。在这篇综述中，我着重于脂质促进孔隙形成的方式，并将其与脂质在膜融合和裂变事件中被吸收的方式进行对比。存在多种涉及脂质的孔隙形成机制，但它们一致导致稳定的混合蛋白脂质结构。这些结构通过形成孔的蛋白质改变脂质膜的固有能力来对环境做出反应，改变形状和/或相位，并直接结合单个脂质分子的机制来稳定。相比之下，尽管融合蛋白类型多样，但膜融合的机制彼此相当相似，绘制了从成对分离的室到完全融合的融合膜的途径。融合蛋白在此过程中产生亚稳结构，就像长期存在的蛋白脂质孔隙形成复合物一样，依赖于脂质双分子层的基本物理性质。膜裂变涉及类似的中间产物，但顺序相反。我的结论是考虑到至少一些成孔蛋白和融合蛋白在进化上是同源的可能性。本文是由Mauro Dalla Serra和Franco Gambale编辑的题为“孔隙形成毒素”的特刊的一部分。(C) 2015 Elsevier B.V.版权所有
Pore-forming proteins and peptides act on their targeted lipid bilayer membranes to increase permeability. This approach to the modulation of biological function is relevant to a great number of living processes, including; infection, parasitism, immunity, apoptosis, development and neurodegeneration. While some pore-forming proteins/peptides assemble into rings of subunits to generate discrete, well-defined pore-forming structures, an increasing number is recognised to form pores via mechanisms which co-opt membrane lipids themselves. Among these, membrane attack complex-perforin/cholesterol-dependent cytolysin (MACPF/CDC) family proteins, Bax/colidn family proteins and actinoporins are especially prominent and among the mechanisms believed to apply are the formation of non-lamellar (semi-toroidal or toroidal) lipidic structures. In this review I focus on the ways in which lipids contribute to pore formation and contrast this with the ways in which lipids are co-opted also in membrane fusion and fission events. A variety of mechanisms for pore formation that involve lipids exists, but they consistently result in stable hybrid proteolipidic structures. These structures are stabilised by mechanisms in which pore forming proteins modify the innate capacity of lipid membranes to respond to their environment, changing shape and/or phase and binding individual lipid molecules directly. In contrast, and despite the diversity in fusion protein types, mechanisms for membrane fusion are rather similar to each other, mapping out a pathway from pairs of separated compartments to fully confluent fused membranes. Fusion proteins generate metastable structures along the way which, like long-lived proteolipidic pore-forming complexes, rely on the basic physical properties of lipid bilayers. Membrane fission involves similar intermediates, in the reverse order. I conclude by considering the possibility that at least some pore-forming and fusion proteins are evolutionarily related homologues. 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.