Raft Trafficking of AB5 Subunit Bacterial Toxins

Biochim Biophys Acta. 2005 Dec 30;1746(3):314-21. doi: 10.1016/j.bbamcr.2005.07.007. Epub 2005 Aug 15.

Abstract

Cholera and the related AB(5)-subunit toxins co-opt plasma membrane (PM) glycolipids to move retrograde into the endoplasmic reticulum (ER) of the host cell where a portion of the toxin is retro-translocated to the cytosol to induce disease. Only glycolipids that associate strongly with detergent insoluble membrane microdomains can sort the toxins backwards from PM to ER. The way certain lipids and proteins are clustered in the plane of the membrane to form lipid rafts likely explains how the glycolipids can function as sorting motifs for the toxins.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Bacterial Toxins / metabolism*
  • Cell Membrane / metabolism
  • Ceramides / metabolism
  • Cholera Toxin / metabolism
  • Endocytosis / physiology*
  • Endoplasmic Reticulum / metabolism
  • Glycolipids / metabolism
  • Golgi Apparatus / metabolism
  • Humans
  • Membrane Lipids / metabolism
  • Membrane Microdomains / metabolism*
  • Membrane Proteins / metabolism
  • Polyomavirus / metabolism
  • Protein Subunits / metabolism
  • Protein Transport
  • Simian virus 40 / metabolism

Substances

  • Bacterial Toxins
  • Ceramides
  • Glycolipids
  • Membrane Lipids
  • Membrane Proteins
  • Protein Subunits
  • Cholera Toxin