Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1

• Published in: The EMBO journal Vol. 34; no. 22; pp. 2840 - 2861
• Main Authors: Lai, Yu-Chiang, Kondapalli, Chandana, Lehneck, Ronny, Procter, James B, Dill, Brian D, Woodroof, Helen I, Gourlay, Robert, Peggie, Mark, Macartney, Thomas J, Corti, Olga, Corvol, Jean-Christophe, Campbell, David G, Itzen, Aymelt, Trost, Matthias, Muqit, Miratul MK
• Format: Journal Article
• Language: English
• Published: London Blackwell Publishing Ltd 12.11.2015; Nature Publishing Group UK; EMBO Press; John Wiley and Sons Inc
• Subjects: Amino Acid Substitution; Biochemistry, Molecular Biology; EMBO20; EMBO22; EMBO31; Enzyme Activation - genetics; Enzymes; Germinal Center Kinases; HEK293 Cells; HeLa Cells; Humans; Life Sciences; Mutation; Mutation, Missense; Oncogene Proteins - genetics; Oncogene Proteins - metabolism; Parkinson's disease; Parkinsonian Disorders - genetics; Parkinsonian Disorders - metabolism; Parkinsonian Disorders - pathology; phosphoproteomics; Phosphorylation; Phosphorylation - genetics; PINK1; Protein Kinases - genetics; Protein Kinases - metabolism; Protein Serine-Threonine Kinases - genetics; Protein Serine-Threonine Kinases - metabolism; Proteomics; rab GTP-Binding Proteins - genetics; rab GTP-Binding Proteins - metabolism; Rab GTPases; Resource; phosphoproteomics; PINK1; Parkinson's disease; Rab GTPases; Rab GTPases Subject Categories Membrane & Intracellular Transport; Post-translational Modifications; Methods & Resources; Proteolysis & Proteomics

Mutations in the PTEN‐induced kinase 1 (PINK1) are causative of autosomal recessive Parkinson's disease (PD). We have previously reported that PINK1 is activated by mitochondrial depolarisation and phosphorylates serine 65 (Ser 65 ) of the ubiquitin ligase Parkin and ubiquitin to stimulate Park...