Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes

Cell. 1991 Nov 1;67(3):591-600. doi: 10.1016/0092-8674(91)90533-5.


Brefeldin A (BFA) is a fungal metabolite that causes a redistribution of the stacked cisternae of the Golgi complex into the endoplasmic reticulum by inhibiting anterograde transport. We report that BFA also causes membrane tubules derived from the trans-Golgi network (TGN) to fuse with early endosomes. In the presence of BFA, a mannose-6-phosphate receptor (M6PR)-enriched tubular network rapidly forms from the TGN, not from the prelysosomal compartment, and can be labeled with endocytic tracers after only 5 min of uptake at either 20 degrees C or 37 degrees C, indicating that it is also functionally an early endosome. Formation of the TGN-early endosome network is microtubule dependent and may involve modification of membrane processes affected by microtubule-associated motor activity. Concomitant with the formation of the fused TGN-early endosome network, there is a greater than 5-fold increase in cell surface M6PRs. The data suggest that BFA has revealed a membrane transport cycle between the TGN and early endosomes, perhaps used for the secretion or delivery of molecules to the cell surface.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Brefeldin A
  • Cell Line
  • Cell Membrane / metabolism
  • Cyclopentanes / pharmacology*
  • Dogs
  • Endocytosis*
  • Fluorescent Antibody Technique
  • Golgi Apparatus / drug effects*
  • Intracellular Membranes / drug effects
  • Intracellular Membranes / ultrastructure
  • Membrane Fusion / drug effects*
  • Microscopy, Electron
  • Microtubules / physiology*
  • Mucolipidoses / physiopathology
  • Rats
  • Receptor, IGF Type 2
  • Receptors, Cell Surface / metabolism


  • Cyclopentanes
  • Receptor, IGF Type 2
  • Receptors, Cell Surface
  • Brefeldin A