Letter abstract
Nature Cell Biology 8, 1376 - 1382 (2006)
Published online: 5 November 2006 | doi:10.1038/ncb1503
Key components of the fission machinery are interchangeable
Jia-Shu Yang1, Leiliang Zhang1, Stella Y. Lee1, Helge Gad2, Alberto Luini2 & Victor W. Hsu1
Brefeldin-A ADP-ribosylated substrate (BARS) and dynamin function in membrane fission in distinct intracellular transport pathways1, 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)2, 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 complex3, 4, 5, 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.
- Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.
- Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy.
Correspondence to: Victor W. Hsu1 e-mail: vhsu@rics.bwh.harvard.edu
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