More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes

Ros, Uris; García‐Sáez, Ana J.

doi:10.1007/s00232-015-9820-y

Cited by 70 publications

(73 citation statements)

References 114 publications

(241 reference statements)

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“…However, it now appears that Bax/Bak oligomerization is the key step in the formation of the apoptotic pore in the membrane for the permeabilization (Garcia-Saez 2012). The formation of this apoptotic pore is also evident from the liposome permeabilization of the model mitochondrial outer membrane induced by Bcl-2 family proteins (Baines et al 2007;Bleicken et al 2016;Garcia-Saez 2014, 2017;García-Sáez et al 2011;Kushnareva et al 2012;Ros and García-Sáez 2015;Shamas-Din et al 2015;Tait and Green 2010).…”

Section: Bcl-2 Protein-mediated Mitochondrial Outer Membrane Permeabimentioning

confidence: 96%

“…5a). A small hydrophobic region in each of the protein monomers is involved in the oligomerization to provide a larger hydrophobic region which can then be inserted into the membrane (Ros and García-Sáez 2015). However, proteins such as colicin and diphtheria toxin of the poreforming protein family can insert their central α-helical hairpin into the membrane and form a proteinaceous pore (Westphal et al 2011).…”

Section: The Structure Of the Apoptotic Porementioning

confidence: 99%

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Mitochondrial outer membrane permeabilization: a focus on the role of mitochondrial membrane structural organization

et al. 2017

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Apoptosis is important in regulating cell death turnover and is mediated by the intrinsic and death receptor-based extrinsic pathways which converge at the mitochondrial outer membrane (MOM) leading to mitochondrial outer membrane permeabilization (MOMP). MOMP results in the release of apoptotic proteins that further activate the downstream pathway of apoptosis. Thus, tight regulation of MOMP is crucial in controlling apoptosis, and a lack of control may lead to tissue and organ malformation and the development of cancers. Despite a growing number of studies focusing on the structure and activity of the proteins involved in mediating MOMP, such as the Bcl-2 family proteins, the mechanism of MOMP is not well understood. In particular, the crucial role of the various structural properties and changes in lipid components of the MOM in mediating the recruitment and activation of different Bcl-2 proteins remains poorly understood. Furthermore, the factors that control the changes in mitochondrial membrane integrity from the initiation to the final disruption of MOM have yet to be clearly defined. In this review, we provide an overview of studies that focus on the mitochondrial membrane with a biophysical analysis of the interactions of the Bcl-2 proteins with the mitochondrial membrane.

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Section: Bcl-2 Protein-mediated Mitochondrial Outer Membrane Permeabimentioning

confidence: 96%

Section: The Structure Of the Apoptotic Porementioning

confidence: 99%

Mitochondrial outer membrane permeabilization: a focus on the role of mitochondrial membrane structural organization

et al. 2017

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“…Membrane manipulation is not limited to physical and chemical procedures conducted on the bilayer itself, but now include alterations to membrane-incorporated channels, such as channel forming substances, which may deform the membrane upon channel formation. [80][81][82] Our picture of channel-membrane interplay is more and more realistic through touching the membrane and designing more sophisticated membranes.…”

Section: Conclusion: Channel-membrane Inter-playmentioning

confidence: 99%

Lipid Bilayers Manipulated through Monolayer Technologies for Studies of Channel-Membrane Interplay

Oiki

Iwamoto

2018

Biological & Pharmaceutical Bulletin

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Fluidity and mosaicity are two critical features of biomembranes, by which membrane proteins function through chemical and physical interactions within a bilayer. To understand this complex and dynamic system, artificial lipid bilayer membranes have served as unprecedented tools for experimental examination, in which some aspects of biomembrane features have been extracted, and to which various methodologies have been applied. Among the lipid bilayers involving liposomes, planar lipid bilayers and nanodiscs, recent developments of lipid bilayer methods and the results of our channel studies are reviewed herein. Principles and techniques of bilayer formation are summarized, which have been extended to the current techniques, where a bilayer is formed from lipid-coated water-in-oil droplets (water-in-oil bilayer). In our newly developed method, termed the contact bubble bilayer (CBB) method, a water bubble is blown from a pipette into a bulk oil phase, and monolayer-lined bubbles are docked to form a bilayer through manipulation by pipette. An asymmetric bilayer can be readily formed, and changes in composition in one leaflet were possible. Taking advantage of the topological configuration of the CBB, such that the membrane's hydrophobic interior is contiguous with the surrounding bulk organic phase, oil-dissolved substances such as cholesterol were delivered directly to the bilayer interior to perfuse around the membrane-embedded channels (membrane perfusion), and current recordings in the single-channel allowed detection of immediate changes in the channels' response to cholesterol. Chemical and mechanical manipulation in each monolayer (monolayer technology) allows the examination of dynamic channel-membrane interplay.

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“…Despite the great diversity of PFT in terms of source, structure or physiological role, they all follow a similar mode of action (Bischofberger et al 2012;Ros and Garcia-Saez 2015). PFT are produced as soluble molecules and then become membrane-associated proteins forming water-filled pores in the membrane of the target cells that disrupt cell homeostasis through the increase of the non-selective passage of molecules.…”

Section: Cellular Mechanisms Triggered Upon Sts-membrane Interaction:mentioning

confidence: 99%

Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone

et al. 2017

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Actinoporins constitute a unique class of poreforming toxins found in sea anemones that are able to bind and oligomerize in membranes, leading to cell swelling, impairment of ionic gradients and, eventually, to cell death. In this review we summarize the knowledge generated from the combination of biochemical and biophysical approaches to the study of sticholysins I and II (Sts, StI/II), two actinoporins largely characterized by the Center of Protein Studies at the University of Havana during the last 20 years. These approaches include strategies for understanding the toxin structure-function relationship, the protein-membrane association process leading to pore formation and the interaction of toxin with cells. The rational combination of experimental and theoretical tools have allowed unraveling, at least partially, of the complex mechanisms involved in toxin-membrane interaction and of the molecular pathways triggered upon this interaction. The study of actinoporins is important not only to gain an understanding of their biological roles in anemone venom but also to investigate basic molecular mechanisms of protein insertion into membranes, protein-lipid interactions and the modulation of protein conformation by lipid binding. A deeper knowledge of the basic molecular mechanisms involved in Sts-cell interaction, as described in this review, will support the current investigations conducted by our group which focus on the design of immunotoxins against tumor cells and antigen-releasing systems to cell cytosol as Stsbased vaccine platforms.

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More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes

Cited by 70 publications

References 114 publications

Mitochondrial outer membrane permeabilization: a focus on the role of mitochondrial membrane structural organization

Mitochondrial outer membrane permeabilization: a focus on the role of mitochondrial membrane structural organization

Lipid Bilayers Manipulated through Monolayer Technologies for Studies of Channel-Membrane Interplay

Biophysical and biochemical strategies to understand membrane binding and pore formation by sticholysins, pore-forming proteins from a sea anemone

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