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J. Cell Biol. 160 (3): 295-296

Copyright © 2003 by the Rockefeller University Press.


Anthrax toxin rafts into cells

Teymuras Kurzchalia

Max-Planck-Institute for Molecular Cell Biology and Genetics, 01307 Dresden, Germany

Address correspondence to Teymuras Kurzchalia, MPI for Cell Biology and Genetics, Pfotenhauerstr. 108, D-01307 Dresden, Germany. Tel.: 49-351-210-2567. Fax: 49-351-210-2000. E-mail: kurzchalia{at}

Abstract: Anthrax toxin binds to a plasma membrane receptor and after endocytosis exerts its deadly effects on the cell. Until now, however, the mechanism of initial toxin uptake was unknown. In this issue, Abrami et al. (2003) demonstrate that toxin oligomerization clusters the anthrax receptor into lipid rafts and this complex is internalized via the clathrin-dependent pathway.

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER.
D. T. Browman, M. E. Resek, L. D. Zajchowski, and S. M. Robbins (2006)
J. Cell Sci. 119, 3149-3160
   Abstract »    Full Text »    PDF »
ATR/TEM8 is highly expressed in epithelial cells lining Bacillus anthracis' three sites of entry: implications for the pathogenesis of anthrax infection.
G. Bonuccelli, F. Sotgia, P. G. Frank, T. M. Williams, C. J. de Almeida, H. B. Tanowitz, P. E. Scherer, K. A. Hotchkiss, B. I. Terman, B. Rollman, et al. (2005)
Am J Physiol Cell Physiol 288, C1402-C1410
   Abstract »    Full Text »    PDF »

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