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Vol. 15, Issue 8, 3631-3641, August 2004

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Cholera Toxin Toxicity Does Not Require Functional Arf6- and Dynamin-dependent Endocytic Pathways

Ramiro H. Massol ^*, Jakob E. Larsen ^*, Yukako Fujinaga , Wayne I. Lencer , and Tomas Kirchhausen ^* 

^* Department of Cell Biology, Harvard Medical School and The Center for Blood Research for Biomedical Research, Boston, Massachusetts 02115; Gastrointestinal Cell Biology, Department of Pediatrics, Children's Hospital and Harvard Medical School and the Harvard Digestive Diseases Center, Boston, Massachusetts 02115

Submitted April 5, 2004; Accepted April 29, 2004
Monitoring Editor: Suzanne Pfeffer

Cholera toxin (CT) and related AB₅ toxins bind to glycolipids at the plasma membrane and are then transported in a retrograde manner, first to the Golgi and then to the endoplasmic reticulum (ER). In the ER, the catalytic subunit of CT is translocated into the cytosol, resulting in toxicity. Using fluorescence microscopy, we found that CT is internalized by multiple endocytic pathways. Inhibition of the clathrin-, caveolin-, or Arf6-dependent pathways by overexpression of appropriate dominant mutants had no effect on retrograde traffic of CT to the Golgi and ER, and it did not affect CT toxicity. Unexpectedly, when we blocked all three endocytic pathways at once, although fluorescent CT in the Golgi and ER became undetectable, CT-induced toxicity was largely unaffected. These results are consistent with the existence of an additional retrograde pathway used by CT to reach the ER.

Online version of this article contains supporting material. Online version is available at www.molbiolcell.org.

Corresponding author. E-mail address: kirchhausen{at}crystal.harvard.edu.

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