Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 49K) Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Kurzchalia, T. Search for Related Content PubMed PubMed Citation Articles by Kurzchalia, T. Social Bookmarking                            What's this?

© The Rockefeller University Press, 0021-9525/2003/2/295 $5.00
The Journal of Cell Biology, Volume 160, Number 3, 295-296

Anthrax toxin rafts into cells

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}mpi-cbg.de

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.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Facebook

Reddit

Technorati

Twitter

This article has been cited by other articles:

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

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents