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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.

Author information

1
Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. Electronic address: gilbert@strubi.ox.ac.uk.
2
Consiglio Nazionale delle Ricerche, Istituto di Biofisica and Fondazione Bruno Kessler, Via alla Cascata 56/C, 38123, Trento, Italy.
3
NorthShore University Health Systems Research Institute and University of Chicago, Evanston, IL 60201, USA.
4
Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK.
5
Department of Biology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia; National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia. Electronic address: gregor.anderluh@ki.si.

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.

KEYWORDS:

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

PMID:
25440714
DOI:
10.1016/j.tibs.2014.09.002
[Indexed for MEDLINE]

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