LRRK2 interacts with ArfGAP1 in mammalian cells and <i>in vivo</i>.

<p>(A) YFP-tagged ArfGAP1 (WT or ΔN) interacts with full-length FLAG-tagged LRRK2 following immunoprecipitation (IP) with anti-FLAG antibody from HEK-293T cells. Domain organization of ArfGAP1 constructs is indicated. (B) Interaction of ArfGAP1-YFP (WT or ΔN) and FLAG-LRRK2 following reverse IP with anti-GFP antibody from HEK-293T cells. (C) Domain mapping reveals the interaction of ArfGAP1-YFP with full-length (WT) LRRK2 and residues 480–895 of LRRK2 (fragment F2) following IP with anti-FLAG antibody from HEK-293T cells. Domain organization of LRRK2 deletion mutants is indicated. (D) Myc-α-synuclein fails to interact with ArfGAP1-YFP following IP with anti-myc antibody from HEK-293T cells. (E) LRRK2 interacts with ArfGAP1 in cerebral cortex extracts from WT mice but not LRRK2 knockout (KO) mice following IP with anti-LRRK2 antibody (clone c41-2). (F) ArfGAP1 interacts with LRRK2 in mouse cerebral cortex following IP with anti-ArfGAP1 antibody but not with a rabbit IgG control. IgG light chain (LC) indicates the equivalent amounts of IgG used for IP. Molecular mass markers are indicated in kilodalton (kDa). Data are representative of at least two independent experiments.