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. Author manuscript; available in PMC: 2018 Jul 10.
Published in final edited form as: Sci Transl Med. 2018 Jan 10;10(423):eaai7795. doi: 10.1126/scitranslmed.aai7795

Figure 4. Effect of LRRK2 mutations on protein kinase activity and GTPase activity.

Figure 4

(A)Schematic representation of LRRK2 domain structure and the respective locations of the N551K, R1398H, and N2081D amino acid substitutions relative to the previously reported PD-associated G2019S mutation and CD-associated M2397T mutation. (B) Representative immunoblot (left panel) and quantification (right panel) of Rab10 phosphorylation by wild-type (WT) and LRRK2 variants in patient macrophages in vitro. (C) GTPase activity of WT and LRRK2 variants. Representative GTP hydrolysis assay (left) and the fraction of hydrolyzed GTP (GDP) over bound GTP (right panel). All values represent the mean of 3 independent experiments ± standard error, and significance was calculated by ANOVA. *P≤0.05, **P≤0.01.ARM, armadillo; ANK, ankyrin repeat region; LRR, leucine-rich repeat; Roc, Ras in complex protein; COR, C terminal of Roc; MAPKKK, MAP kinase kinase kinase, WD40, WD40 protein-protein interaction domain.