Additional file 1: Figure S1. of Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation

Distinct pathogenic LRRK2 mutants cause deficits in centrosome cohesion in transfected HEK293T cells. (DOCX 1160 kb

Additional file 3: Figure S3. of Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation

LRRK2 phosphorylates Rab8a at T72, and phosphomimetic mutants do not display altered nucleotide binding or retention. (DOCX 1005 kb

Additional file 5: Figure S5. of Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation

Golgi dispersal/disruption has no effect on LRRK2-mediated pericentrosomal/centrosomal accumulation of Rab8a. (DOCX 1670 kb

Additional file 6: Figure S6. of Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation

Rab8a protein levels and pericentrosomal/centrosomal accumulation of phosphorylated Rab8a in lymphoblasts from control and G2019S mutant LRRK2 PD patients. (DOCX 636 kb

Additional file 2: Figure S2. of Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation

Pathogenic LRRK2 disturbs centrosome cohesion in a kinase-dependent manner. (DOCX 1155 kb

Additional file 4: Figure S4. of Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation

Differential interactions of wildtype and phospho-mimetic Rab8a mutants with GDI1/2 and Rabin8, effects on centrosome splitting and subcellular localization. (DOCX 824 kb