Ontology highlight
ABSTRACT:
SUBMITTER: Malik AU
PROVIDER: S-EPMC7886321 | biostudies-literature | 2021 Feb
REPOSITORIES: biostudies-literature
Malik Asad U AU Karapetsas Athanasios A Nirujogi Raja S RS Mathea Sebastian S Chatterjee Deep D Pal Prosenjit P Lis Pawel P Taylor Matthew M Purlyte Elena E Gourlay Robert R Dorward Mark M Weidlich Simone S Toth Rachel R Polinski Nicole K NK Knapp Stefan S Tonelli Francesca F Alessi Dario R DR
The Biochemical journal 20210201 3
Autosomal dominant mutations in LRRK2 that enhance kinase activity cause Parkinson's disease. LRRK2 phosphorylates a subset of Rab GTPases including Rab8A and Rab10 within its effector binding motif. Here, we explore whether LRRK1, a less studied homolog of LRRK2 that regulates growth factor receptor trafficking and osteoclast biology might also phosphorylate Rab proteins. Using mass spectrometry, we found that in LRRK1 knock-out cells, phosphorylation of Rab7A at Ser72 was most impacted. This r ...[more]