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. Author manuscript; available in PMC: 2008 Nov 25.
Published in final edited form as: J Neurosci Res. 2008 Jun;86(8):1711–1720. doi: 10.1002/jnr.21622

Fig. 3. Wild-type and the R1441C pathogenic mutant of LRRK2 selectively interact with α/β-tubulin heterodimers.

Fig. 3

(A) Western blot analysis of LRRK2 co-precipitation assay. FLAG-tagged wild-type and mutant LRRK2 proteins were overexpressed in HEK293T cells and immunoprecipitated with anti-LRRK2 coupled to Dynabeads. Immunoprecipitates were separated by 6% Tris-glycine SDS-PAGE, electrophoretically transferred to PVDF and Western blotted with FLAG, α-tubulin and β-tubulin antibodies. Control refers to untransfected cells. The Western blots shown are representative of three independent experiments. (B) Quantification of Western blot analysis of LRRK2 co-precipitation assay. FLAG, α-tubulin and β-tubulin Western blots were quantified by densitometry and the percentage of α/β-tubulin bound was normalized to LRRK2-FLAG protein expression levels. Error bars represent SEM for three independent experiments. n.s. is non-significant as assessed by a two-tailed unpaired Student’s t-test.