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MBC in Press, published online ahead of print May 14, 2004
Mol. Biol. Cell 10.1091/mbc.E04-04-0283

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Submitted on April 5, 2004
Revised on April 29, 2004
Accepted on April 29, 2004

Cholera Toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways

Ramiro H. Massol{dagger}, Jakob E. Larsen{dagger}, Yukako Fujinaga{ddagger}, Wayne I. Lencer{ddagger}, and Tomas Kirchhausen{dagger}*

{dagger}Department of Cell Biology, Harvard Medical School and The CBR Institute for Biomedical Research, Boston, MA; {ddagger}Gastrointestinal Cell Biology, Department of Pediatrics, Children's Hospital and Harvard Medical School and the Harvard Digestive Diseases Center, Boston, MA

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 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.

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




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