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      Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation 

      Madero-Pérez, Jesús; Fernández, Elena; Fernández, Belén; Lara Ordóñez, Antonio J.; Ramírez, Marian Blanca; Gómez-Suaga, Patricia; Waschbüsch, Dieter; Lobbestael, Evy; Baekelandt, Veerle; Nairn, Angus C.; Ruiz-Martínez, Javier; Aiastui, Ana; López de Munain Arregui, Adolfo José; Lis, Pawel; Comptdaer, Thomas; Taymans, Jean-Marc; Chartier-Harlin, Marie-Christine; Beilina, Alexandria; Gonnelli, Adriano; Cookson, Mark R.; Greggio, Elisa; Hilfiker, Sabine (Biomed Central, 2019-01-23)
      Background: Mutations in LRRK2 are a common genetic cause of Parkinson's disease (PD). LRRK2 interacts with and phosphorylates a subset of Rab proteins including Rab8a, a protein which has been implicated in various ...
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      Pathogenic LRRK2 regulates centrosome cohesion via Rab10/RILPL1-mediated CDK5RAP2 displacement 

      Fernández, Elena; Madero-Pérez, Jesús; Lara Ordóñez, Antonio J.; Naaldijk, Yahaira; Fasiczka, Rachel; Aiastui, Ana; Ruiz-Martínez, Javier; López de Munain Arregui, Adolfo José; Cowley, Sally A.; Wade-Martins, Richard; Hilfiker, Sabine (Cell Press, 2022-06-17)
      Mutations in LRRK2 increase its kinase activity and cause Parkinson's disease. LRRK2 phosphorylates a subset of Rab proteins which allows for their binding to RILPL1. The phospho-Rab/RILPL1 interaction causes deficits in ...