Key components of the fission machinery are interchangeable.
Brefeldin-A ADP-ribosylated substrate (BARS) and dynamin function in membrane fission in distinct intracellular transport pathways, but whether their functions are mechanistically similar is unclear. Here, we show that ARFGAP1, a GTPase-activating protein (GAP) for ADP-ribosylation factor 1 (ARF1), couples to either BARS or endophilin B for vesicle formation by the coat protein I (COPI) complex - a finding that reveals an unanticipated mechanistic flexibility in mammalian COPI transport. Because dynamin is coupled to endophilin A in vesicle formation by the clathrin-coat complex, our finding also predicts that dynamin and ARF GAPs are likely to be functional counterparts in membrane fission among different transport pathways that connect intracellular membrane compartments.
Yang
Jia-Shu
JS
Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.
Zhang
Leiliang
L
Lee
Stella Y
SY
Gad
Helge
H
Luini
Alberto
A
Hsu
Victor W
VW
D000217:Acyltransferases / Q000378:metabolism; D000818:Animals; D020755:Coat Protein Complex I / Q000378:metabolism; D018699:Coated Vesicles / Q000378:metabolism; D004622:Embryo, Mammalian / Q000166:cytology; D005347:Fibroblasts / Q000166:cytology; D006056:Golgi Apparatus / Q000648:ultrastructure; D007425:Intracellular Membranes / Q000378:metabolism* / Q000648:ultrastructure; D051379:Mice; D014157:Transcription Factors / Q000378:metabolism
D020755:Coat Protein Complex I; D014157:Transcription Factors; D000217:Acyltransferases; C018764:2-acylglycerophosphate acyltransferase