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Trends Biochem Sci. 2014 Nov;39(11):510-6. doi: 10.1016/j.tibs.2014.09.002. Epub 2014 Oct 19.

Membrane pore formation at protein-lipid interfaces.

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Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. Electronic address:
Consiglio Nazionale delle Ricerche, Istituto di Biofisica and Fondazione Bruno Kessler, Via alla Cascata 56/C, 38123, Trento, Italy.
NorthShore University Health Systems Research Institute and University of Chicago, Evanston, IL 60201, USA.
Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK.
Department of Biology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia; National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia. Electronic address:


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.


Bcl-2/colicin family proteins; MACPF/CDC family proteins; actinoporins; pore-forming peptides and proteins; protein–membrane interactions; toroidal pore formation

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