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. 2013 Nov 25;289(2):895–908. doi: 10.1074/jbc.M113.507913

FIGURE 8.

FIGURE 8.

LRRK2 Roc domain autophosphorylation interferes with the LRRK2-tubulin interaction. A, Western blot showing a decrease of the LRRK2-β-tubulin interaction in co-immunoprecipitation experiments with the G2019S mutant in comparison with wild-type LRRK2 (black box). This decrease was rescued by LRRK2 kinase inhibition with LRRK2in1. B–D, quantitative YTH assays show that the introduction of phosphomimetic mutations at Roc domain autophosphorylation sites decreases the interaction with TUBB4 (B) and TUBB (C) but has no effect on RocCOR dimerization (D). Introduction of an alanine at the autophosphorylation sites has less and more diverse effects on the interactions shown. *, p < 0.05; **, p < 0.01; ***, p < 0.001; n = 5–6.