A Pore-forming Toxin Interacts with a GPI-anchored Protein and Causes Vacuolation of the Endoplasmic Reticulum

• DOI: 10.1083/jcb.140.3.525
• Publication Date: 2002-07-26T16:47:50Z
• Authors: Laurence Abrami; Marc Fivaz; Pierre-Etienne Gl...; Robert G. Parton; F. van der Goot
• Keywords: Aerolysin; Cholera toxin; Lipid raft; Membrane contact site; Cell membrane

In this paper, we have investigated the effects of pore-forming toxin aerolysin, produced by Aeromonas hydrophila, on mammalian cells. Our data indicate that protoxin binds to an 80-kD glycosyl-phosphatidylinositol (GPI)-anchored protein BHK cells, and bound is associated with specialized plasma membrane domains, described as detergent-insoluble microdomains, or cholesterol-glycolipid “rafts.” We show then processed its mature form host cell proteases. propose preferential association rafts, through binding GPI-anchored proteins, likely increase local concentration thereby promote oligomerization, a step it prerequisite for channel formation. formation does not lead disruption but selective permeabilization small ions such potassium, which causes depolarization. Next studied consequences organization dynamics intracellular membranes. Strikingly, found dramatic vacuolation ER, affect other compartments. Concomitantly find COPI coat released from biosynthetic membranes transport newly synthesized transmembrane G vesicular stomatitis virus inhibited. proaerolysin proteins processing oligomerization in membrane, turn disorganization early dynamics.