Abstract
Pore-forming proteins (PFPs) punch holes in their target cell membrane to alter their permeability. Permeabilization of lipid membranes by PFPs has received special attention to study the basic molecular mechanisms of protein insertion into membranes and the development of biotechnological tools. PFPs act through a general multi-step mechanism that involves (i) membrane partitioning, (ii) insertion into the hydrophobic core of the bilayer, (iii) oligomerization, and (iv) pore formation. Interestingly, PFPs and membranes show a dynamic interplay. As PFPs are usually produced as soluble proteins, they require a large conformational change for membrane insertion. Moreover, membrane structure is modified upon PFPs insertion. In this context, the toroidal pore model has been proposed to describe a pore architecture in which not only protein molecules but also lipids are directly involved in the structure. Here, we discuss how PFPs and lipids cooperate and remodel each other to achieve pore formation, and explore new evidences of protein-lipid pore structures.
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Abbreviations
- PFPs:
-
Pore-forming proteins
- PFTs:
-
Pore-forming toxins
- CDCs:
-
Cholesterol-dependent cytolysins
- Chol:
-
Cholesterol
- AMPs:
-
Antimicrobial peptides
- SM:
-
Sphingomyelin
- CL:
-
Cardiolipin
- PC:
-
Phosphatidylcholine
- PE:
-
Phosphatidylethanolamine
- GPI:
-
Glycosylphosphatidylinositol
- MACPF/CDC:
-
Complex-perforin/cholesterol-dependent cytolysin
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Acknowledgments
We are very grateful to Dr. Katia Cosentino, Raquel Salvador Gallego, Lohans Pedrera Puentes, and Dr. Yuri Quintana Pacheco for critically reading of the manuscript. U.R. acknowledges funding support from the Max Planck Society to visit the Membrane Biophysics lab at IFIB, Tübingen University, Tübingen, Germany.
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Ros, U., García-Sáez, A.J. More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes. J Membrane Biol 248, 545–561 (2015). https://doi.org/10.1007/s00232-015-9820-y
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DOI: https://doi.org/10.1007/s00232-015-9820-y