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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.

Original publication

DOI

10.1016/j.tibs.2014.09.002

Type

Journal article

Journal

Trends Biochem Sci

Publication Date

11/2014

Volume

39

Pages

510 - 516

Keywords

Bcl-2/colicin family proteins, MACPF/CDC family proteins, actinoporins, pore-forming peptides and proteins, protein–membrane interactions, toroidal pore formation, Cell Membrane, Colicins, Lipid Bilayers, Melitten, Membrane Lipids, Models, Molecular, Pore Forming Cytotoxic Proteins, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary