Article abstract
Nature Cell Biology 7, 570 - 580 (2005)
Published online: 8 May 2005 | doi:10.1038/ncb1260
There is a Corrigendum (June 2005) associated with this Article.
CtBP3/BARS drives membrane fission in dynamin-independent transport pathways
Matteo Bonazzi1,4, Stefania Spanò2,4, Gabriele Turacchio1, Claudia Cericola2, Carmen Valente2, Antonino Colanzi2, Hee Seok Kweon1, Victor W. Hsu3, Elena V. Polishchuck1, Roman S. Polishchuck1, Michele Sallese1, Teodoro Pulvirenti1, Daniela Corda2 & Alberto Luini1
Abstract
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.
- Laboratory of Membrane Traffic, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy.
- Laboratory of Cell Regulation, Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy.
- Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.
- These authors contributed equally to this work.
Correspondence to: Alberto Luini1 e-mail: luini@dcbo.negrisud.it
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