Anno2014
AutoriRobert J.C. Gilbert1, Mauro Dalla Serra2, Christopher J. Froelich3, Mark I. Wallace4,and Gregor Anderluh
AbstractPore-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 A beta 1-41, 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.
RivistaTrends In Biochemical Sciences (amst., Ref. Ed.)
ISSN0376-5067
Impact factor0
Volume39
Pagina inizio510
Pagina fine516
Autori IBFMauro DALLA SERRA
Linee di Ricerca IBFMD.P01.028.001
Sedi IBFIBF.TN