CtBP3/BARS drives membrane fission in dynamin-independent transport pathways

Nat Cell Biol. 2005 Jun;7(6):570-80. doi: 10.1038/ncb1260. Epub 2005 May 8.


Membrane fission is a fundamental step in membrane transport. So far, the only fission protein machinery that has been implicated in in vivo transport involves dynamin, and functions in several, but not all, transport pathways. Thus, other fission machineries may exist. Here, we report that carboxy-terminal binding protein 3/brefeldin A-ribosylated substrate (CtBP3/BARS) controls fission in basolateral transport from the Golgi to the plasma membrane and in fluid-phase endocytosis, whereas dynamin is not involved in these steps. Conversely, CtBP3/BARS protein is inactive in apical transport to the plasma membrane and in receptor-mediated endocytosis, both steps being controlled by dynamin. This indicates that CtBP3/BARS controls membrane fission in endocytic and exocytic transport pathways, distinct from those that require dynamin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COS Cells
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure
  • Chlorocebus aethiops
  • Dogs
  • Dynamins / metabolism*
  • Endocytosis / physiology
  • Exocytosis / physiology
  • Golgi Apparatus / metabolism
  • Golgi Apparatus / ultrastructure
  • Intracellular Membranes / metabolism*
  • Intracellular Membranes / ultrastructure
  • Microscopy, Electron, Transmission
  • Organelles / metabolism*
  • Organelles / ultrastructure
  • Protein Transport / physiology
  • Receptors, Cell Surface / metabolism
  • Transcription Factors / metabolism*
  • Transport Vesicles / metabolism*
  • Transport Vesicles / ultrastructure


  • Carrier Proteins
  • Ctbp1 protein, rat
  • Receptors, Cell Surface
  • Transcription Factors
  • Dynamins