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

Published byΚηφεύς Βιτάλη Modified over 5 years ago

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Presentation on theme: "Fig. 4 Effect of LRRK2 mutations on protein kinase activity and GTPase activity. Effect of LRRK2 mutations on protein kinase activity and GTPase activity."— Presentation transcript:

1 Fig. 4 Effect of LRRK2 mutations on protein kinase activity and GTPase activity.
Effect of LRRK2 mutations on protein kinase activity and GTPase activity. (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) and quantification (right) of Rab10 phosphorylation (pRab10) by wild type (WT) and LRRK2 variants in patient macrophages in vitro. (C) Guanosine triphosphate binding and hydrolyzing enzyme (GTPase) activity of WT and LRRK2 variants. Representative guanosine triphosphate (GTP) hydrolysis assay (left) and the fraction of hydrolyzed GTP (guanosine diphosphate, GDP) over bound GTP (right). All values represent the mean of three independent experiments ± SE, and significance was calculated by analysis of variance (ANOVA). *P ≤ 0.05 and **P ≤ ARM, armadillo; ANK, ankyrin repeat region; LRR, leucine-rich repeat; ROC, Ras of complex proteins; COR, C terminal of ROC; MAPKKK, mitogen-activated protein (MAP) kinase kinase kinase; WD40, WD40 protein-protein interaction domain. Ken Y. Hui et al., Sci Transl Med 2018;10:eaai7795 Published by AAAS

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