Fig. 1
From: Oligomerization of Lrrk controls actin severing and α-synuclein neurotoxicity in vivo
Modulation of Lrrk enhances α-synuclein neurotoxicity in Drosophila. a, Increasing or decreasing Drosophila Lrrk worsens the locomotor climbing defect induced by the expression of transgenic human wild type human α-synuclein, which is further enhanced by expressing mutant forms of Lrrk engineered to mimic Parkinson’s disease mutations. b, Altering Lrrk levels further enhances α-synuclein-mediated loss of hematoxylin-stained neurons in the anterior medulla, as quantified in (c) when compared to flies expressing α-synuclein alone. Scale bar represents 10 µm in (b). d, Increasing or decreasing Lrrk levels also further decreases the α-synuclein-induced loss of tyrosine hydroxylase-positive neurons in the anterior medulla (arrows), as quantified in (e) when compared to flies expressing α-synuclein alone. Scale bar represents 5 µm in (d). f, Western blotting reveals no change in α-synuclein levels with manipulation of Lrrk. The blot is reprobed for GAPDH to illustrate equivalent protein loading. Lrrk-: Lrrke03680. Lrrk-WT: wild type Lrrk overexpression. Y1383C, I1915T and GS are Lrrk mutants homologous to Parkinson’s disease-associated human LRRK2 mutants Y1699C, I2020T, and G2019S respectively. n=6 per genotype. Data are represented as mean ± SD. *p<0.05, **p<0.01, ***p<0.005, ANOVA with Bonferroni post-test analysis. Control is nSyb-GAL4, nSybQF2/+. Flies are 10 days old in (a-d) and 1 day old in (f)