title: CtBP3/BARS drives membrane fission in dynamin-independent transport pathways.
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.
authors.affiliation: Laboratory of Membrane Traffic, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy.
authors.forename: Matteo
authors.initials: M
authors.lastname: Bonazzi
authors.forename: Stefania
authors.initials: S
authors.lastname: Spanò
authors.forename: Gabriele
authors.initials: G
authors.lastname: Turacchio
authors.forename: Claudia
authors.initials: C
authors.lastname: Cericola
authors.forename: Carmen
authors.initials: C
authors.lastname: Valente
authors.forename: Antonino
authors.initials: A
authors.lastname: Colanzi
authors.forename: Hee Seok
authors.initials: HS
authors.lastname: Kweon
authors.forename: Victor W
authors.initials: VW
authors.lastname: Hsu
authors.forename: Elena V
authors.initials: EV
authors.lastname: Polishchuck
authors.forename: Roman S
authors.initials: RS
authors.lastname: Polishchuck
authors.forename: Michele
authors.initials: M
authors.lastname: Sallese
authors.forename: Teodoro
authors.initials: T
authors.lastname: Pulvirenti
authors.forename: Daniela
authors.initials: D
authors.lastname: Corda
authors.forename: Alberto
authors.initials: A
authors.lastname: Luini
mesh_terms: D000818:Animals; D019556:COS Cells; D002352:Carrier Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D002522:Chlorocebus aethiops; D004285:Dogs; D034281:Dynamins / Q000378:metabolism*; D004705:Endocytosis / Q000502:physiology; D005089:Exocytosis / Q000502:physiology; D006056:Golgi Apparatus / Q000378:metabolism / Q000648:ultrastructure; D007425:Intracellular Membranes / Q000378:metabolism* / Q000648:ultrastructure; D046529:Microscopy, Electron, Transmission; D015388:Organelles / Q000378:metabolism* / Q000648:ultrastructure; D021381:Protein Transport / Q000502:physiology; D011956:Receptors, Cell Surface / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D022161:Transport Vesicles / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D002352:Carrier Proteins; C119945:Ctbp1 protein, rat; D011956:Receptors, Cell Surface; D014157:Transcription Factors; D034281:Dynamins