Structural basis for the binding of tryptophan-based motifs by δ-COP.
Cambridge, United Kingdom. In Proc Natl Acad Sci U S A, Dec 2015
Mutations designed on the basis of the structure in conjunction with isothermal titration calorimetry confirm the mode of binding and show that mammalian δ-COP binds related tryptophan-based motifs such as that from ArfGAP1 in a similar manner.
Interaction of LRRK2 with kinase and GTPase signaling cascades.
Boston, United States. In Front Mol Neurosci, 2013
Binding to GTPases, GTPase-activating proteins and GTPase exchange factors are another strong theme in LRRK2 biology, with LRRK2 binding to rac1, cdc42, rab5, rab7L1, endoA, RGS2, ArfGAP1, and ArhGEF7.
ARFGAP1 promotes AP-2-dependent endocytosis.
Boston, United States. In Nat Cell Biol, 2011
role of ARFGAP1 in AP-2-regulated endocytosis has mechanistic parallels with its roles in COPI transport, as both its GAP activity and coat function contribute to promoting AP-2 transport
Asymmetric tethering of flat and curved lipid membranes by a golgin.
Antibes, France. In Science, 2008
This asymmetric tethering relied on motifs that sensed membrane curvature both in the N terminus of GMAP-210 and in ArfGAP1, which controlled the interaction of the C terminus of GMAP-210 with the small guanine nucleotide-binding protein Arf1.
Key components of the fission machinery are interchangeable.
Boston, United States. In Nat Cell Biol, 2006
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.