A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum

Abrami, L., Fivaz, M., Glauser, P. E., Parton, R. G. and van der Goot, F. G. (1998) A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum. Journal of Cell Biology, 140 3: 525-540. doi:10.1083/jcb.140.3.525

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ249092_OA.pdf Full text (open access) application/pdf 847.41KB 0

Author Abrami, L.
Fivaz, M.
Glauser, P. E.
Parton, R. G.
van der Goot, F. G.
Title A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum
Journal name Journal of Cell Biology   Check publisher's open access policy
ISSN 0021-9525
1540-8140
Publication date 1998-02-01
Year available 1998
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1083/jcb.140.3.525
Open Access Status File (Publisher version)
Volume 140
Issue 3
Start page 525
End page 540
Total pages 16
Place of publication New York, NY, United States
Publisher Rockefeller University Press
Language eng
Abstract In this paper, we have investigated the effects of the pore-forming toxin aerolysin, produced by Aeromonas hydrophila, on mammalian cells. Our data indicate that the protoxin binds to an 80-kD glycosylphosphatidylinositol (GPI)-anchored protein on BHK cells, and that the bound toxin is associated with specialized plasma membrane domains, described as detergent-insoluble microdomains, or cholesterol-glycolipid "rafts." We show that the protoxin is then processed to its mature form by host cell proteases, We propose that the preferential association of the toxin with rafts, through binding to GPI-anchored proteins, is likely to increase the local toxin concentration and thereby promote oligomerization, a step that it is a prerequisite for channel formation, We show that channel formation does not lead to disruption of the plasma membrane but to the selective permeabilization to small ions such as potassium, which causes plasma membrane depolarization. Next we studied the consequences of channel formation on the organization and dynamics of intracellular membranes, Strikingly, we found that the toxin causes dramatic vacuolation of the ER, but does not affect other intracellular compartments, Concomitantly we find that the COPI coat is released from biosynthetic membranes and that biosynthetic transport of newly synthesized transmembrane G protein of vesicular stomatitis virus is inhibited, Our data indicate that binding of proaerolysin to GPI-anchored proteins and processing of the toxin lead to oligomerization and channel formation in the plasma membrane, which in turn causes selective disorganization of early biosynthetic membrane dynamics.
Keyword Staphylococcal Alpha-Toxin
Planar Lipid Bilayers
Aeromonas-Hydrophila
Golgi-Complex
Cell-Surface
Listeria-Monocytogenes
Proteolytic Activation
Erythrocyte-Membranes
Helicobacter-Pylori
Apical Distribution
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 173 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 178 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sat, 10 Sep 2011, 05:54:55 EST by System User on behalf of Scholarly Communication and Digitisation Service