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

被引:137
作者
Bonazzi, M
Spanò, S
Turacchio, G
Cericola, C
Valente, C
Colanzi, A
Kweon, HS
Hsu, VW
Polishchuck, EV
Polishchuck, RS
Sallese, M
Pulvirenti, T
Corda, D
Luini, A [1 ]
机构
[1] Ist Ric Farmacol Mario Negri, Consorzio Mario Negri Sud, Lab Membrane Traff, I-66030 Santa Maria Imbaro, Italy
[2] Ist Ric Farmacol Mario Negri, Consorzio Mario Negri Sud, Lab Cell Regulat, Dept Cell Biol & Oncol, I-66030 Santa Maria Imbaro, Italy
[3] Brigham & Womens Hosp, Div Rheumatol Immunol & Allergy, Boston, MA 02115 USA
[4] Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA
关键词
D O I
10.1038/ncb1260
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:570 / U11
页数:15
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