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

Matteo Bonazzi, Stefania Spanò, Gabriele Turacchio, Claudia Cericola, Carmen Valente, Antonino Colanzi, Hee Seok Kweon, Victor W Hsu, Elena V Polishchuck, Roman S Polishchuck, Michele Sallese, Teodoro Pulvirenti, Daniela Corda, Alberto Luini

Research output: Contribution to journalArticlepeer-review

151 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)570-80
Number of pages11
JournalNature Cell Biology
Issue number6
Publication statusPublished - Jun 2005


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


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