Membrane pore formation at protein-lipid interfaces.

Robert J C Gilbert, Mauro Dalla Serra, Christopher J Froelich, Mark I Wallace, Gregor Anderluh

Journal: Trends in biochemical sciences 2015;39(11):510-6

PMID: 25440714

Full Text on Elsevier Science View on PubMed

Abstract

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.

Address: Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. Electronic address: [email protected].; 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: [email protected].

DOI: 10.1016/j.tibs.2014.09.002

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MeSH Terms: Cell Membrane, Colicins, Lipid Bilayers, Melitten, Membrane Lipids, Models, Molecular, Pore Forming Cytotoxic Proteins, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary