2. Academic Validation
  3. Ganglioside GM1-mediated transcytosis of cholera toxin bypasses the retrograde pathway and depends on the structure of the ceramide domain

Ganglioside GM1-mediated transcytosis of cholera toxin bypasses the retrograde pathway and depends on the structure of the ceramide domain

  • J Biol Chem. 2013 Sep 6;288(36):25804-25809. doi: 10.1074/jbc.M113.474957.
David E Saslowsky 1,  Yvonne M Te Welscher 2,  Daniel J-F Chinnapen 2,  Jessica S Wagner 3,  Joy Wan 4,  Eli Kern 4,  Wayne I Lencer 5
Affiliations

Affiliations

  • 1 From the Division of Gastroenterology, Boston Children's Hospital,; Harvard Digestive Diseases Center, and; Harvard Medical School, Boston, Massachusetts, 02115. Electronic address: david.saslowsky@childrens.harvard.edu.
  • 2 From the Division of Gastroenterology, Boston Children's Hospital,; Harvard Medical School, Boston, Massachusetts, 02115.
  • 3 From the Division of Gastroenterology, Boston Children's Hospital,; Harvard Digestive Diseases Center, and.
  • 4 From the Division of Gastroenterology, Boston Children's Hospital.
  • 5 From the Division of Gastroenterology, Boston Children's Hospital,; Harvard Digestive Diseases Center, and; Harvard Medical School, Boston, Massachusetts, 02115.
PMID: 23884419 DOI: 10.1074/jbc.M113.474957
Abstract

Cholera toxin causes diarrheal disease by binding ganglioside GM1 on the apical membrane of polarized intestinal epithelial cells and trafficking retrograde through sorting endosomes, the trans-Golgi network (TGN), and into the endoplasmic reticulum. A fraction of toxin also moves from endosomes across the cell to the basolateral plasma membrane by transcytosis, thus breeching the intestinal barrier. Here we find that sorting of cholera toxin into this transcytotic pathway bypasses retrograde transport to the TGN. We also find that GM1 sphingolipids can traffic from apical to basolateral membranes by transcytosis in the absence of toxin binding but only if the GM1 species contain cis-unsaturated or short acyl chains in the ceramide domain. We found previously that the same GM1 species are needed to efficiently traffic retrograde into the TGN and endoplasmic reticulum and into the recycling endosome, implicating a shared mechanism of action for sorting by lipid shape among these pathways.

Keywords

Cell Biology; Cholera Toxin; Endosomes; Ganglioside; Intracellular Trafficking; Lipid Transport; Membrane Lipids; Membrane Trafficking; Polarized Epithelia; Sphingolipid.

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