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

Authors :
Bonazzi, Matteo
Spanò, Stefania
Turacchio, Gabriele
Cericola, Claudia
Valente, Carmen
Colanzi, Antonino
Kweon, Hee Seok
Hsu, Victor W.
Polishchuck, Elena V.
Polishchuck, Roman S.
Sallese, Michele
Pulvirenti, Teodoro
Corda, Daniela
Luini, Alberto
Source :
Nature Cell Biology; Jun2005, Vol. 7 Issue 6, p570-580, 11p
Publication Year :
2005

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
14657392
Volume :
7
Issue :
6
Database :
Complementary Index
Journal :
Nature Cell Biology
Publication Type :
Academic Journal
Accession number :
17187557
Full Text :
https://doi.org/10.1038/ncb1260