Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

Originally published as MBC in Press, 10.1091/mbc.E06-04-0310 on August 2, 2006

Vol. 17, Issue 10, 4379-4389, October 2006

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E06-04-0310v1
17/10/4379    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hehnly, H.
Right arrow Articles by Stamnes, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hehnly, H.
Right arrow Articles by Stamnes, M.

Shiga Toxin Facilitates Its Retrograde Transport by Modifying Microtubule DynamicsFormula

Heidi Hehnly*, David Sheff{dagger}, and Mark Stamnes*

Departments of *Physiology and Biophysics and {dagger}Pharmacology, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, IA 52242

Submitted April 17, 2006; Revised July 3, 2006; Accepted July 21, 2006
Monitoring Editor: Adam Linstedt

The bacterial exotoxin Shiga toxin is endocytosed by mammalian host cells and transported retrogradely through the secretory pathway before entering the cytosol. Shiga toxin also increases the levels of microfilaments and microtubules (MTs) upon binding to the cell surface. The purpose for this alteration in cytoskeletal dynamics is unknown. We have investigated whether Shiga toxin-induced changes in MT levels facilitate its intracellular transport. We have tested the effects of the Shiga toxin B subunit (STB) on MT-dependent and -independent transport steps. STB increases the rate of MT-dependent Golgi stack repositioning after nocodazole treatment. It also enhances the MT-dependent accumulation of transferrin in a perinuclear recycling compartment. By contrast, the rate of MT-independent transferrin recycling is not significantly different when STB is present. We found that STB normally requires MTs and dynein for its retrograde transport to the juxtanuclear Golgi complex and that STB increases MT assembly. Furthermore, we find that MT polymerization is limiting for STB transport in cells. These results show that STB-induced changes in cytoskeletal dynamics influence intracellular transport. We conclude that the increased rate of MT assembly upon Shiga toxin binding facilitates the retrograde transport of the toxin through the secretory pathway.

Formula The online version of this contains supplemental material at MBC Online (http://www.molbiolcell.org).

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-04-0310) on August 2, 2006.

Address correspondence to: Mark Stamnes (mark-stamnes{at}uiowa.edu)

Abbreviations used: MT, microtubule; MTOC, microtubule organizing center; STB, Shiga toxin B subunit.




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. L. Torgersen, S. Walchli, S. Grimmer, S. S. Skanland, and K. Sandvig
Protein Kinase C{delta} Is Activated by Shiga Toxin and Regulates Its Transport
J. Biol. Chem., June 1, 2007; 282(22): 16317 - 16328.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2006 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.