Membrane pore formation at protein-lipid interfaces.
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 'proteolipidi...
| Päätekijät: | , , , , |
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| Aineistotyyppi: | Journal article |
| Kieli: | English |
| Julkaistu: |
2014
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| _version_ | 1826305329646796800 |
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| author | Gilbert, R Dalla Serra, M Froelich, C Wallace, M Anderluh, G |
| author_facet | Gilbert, R Dalla Serra, M Froelich, C Wallace, M Anderluh, G |
| author_sort | Gilbert, R |
| collection | OXFORD |
| description | 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 Aβ1-41, 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. |
| first_indexed | 2024-03-07T06:31:15Z |
| format | Journal article |
| id | oxford-uuid:f60f9ca8-13e8-42ff-bc58-26408ee90c7b |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:31:15Z |
| publishDate | 2014 |
| record_format | dspace |
| spelling | oxford-uuid:f60f9ca8-13e8-42ff-bc58-26408ee90c7b2022-03-27T12:32:09ZMembrane pore formation at protein-lipid interfaces.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f60f9ca8-13e8-42ff-bc58-26408ee90c7bEnglishSymplectic Elements at Oxford2014Gilbert, RDalla Serra, MFroelich, CWallace, MAnderluh, GPore-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 Aβ1-41, 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. |
| spellingShingle | Gilbert, R Dalla Serra, M Froelich, C Wallace, M Anderluh, G Membrane pore formation at protein-lipid interfaces. |
| title | Membrane pore formation at protein-lipid interfaces. |
| title_full | Membrane pore formation at protein-lipid interfaces. |
| title_fullStr | Membrane pore formation at protein-lipid interfaces. |
| title_full_unstemmed | Membrane pore formation at protein-lipid interfaces. |
| title_short | Membrane pore formation at protein-lipid interfaces. |
| title_sort | membrane pore formation at protein lipid interfaces |
| work_keys_str_mv | AT gilbertr membraneporeformationatproteinlipidinterfaces AT dallaserram membraneporeformationatproteinlipidinterfaces AT froelichc membraneporeformationatproteinlipidinterfaces AT wallacem membraneporeformationatproteinlipidinterfaces AT anderluhg membraneporeformationatproteinlipidinterfaces |