Proteomics

Dataset Information

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Phosphoproteome of PINK1 in HEK293 cells

ABSTRACT: triple SILAC phosphoproteomics experiment of Flp-In T-Rex HEK293 cells stably expressing either FLAG empty, PINK1-FLAG Kinase dead or PINK1-FLAG wild type were grown in ‘light’ (K0R0), ‘medium’ (K4R6) and ‘heavy’ (K8,R10) SILAC media, respectively.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

DISEASE(S): Parkinson's Disease

SUBMITTER: Matthias Trost  

LAB HEAD: Matthias Trost

PROVIDER: PXD002127 | Pride | 2015-09-16

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
CKondapalli_131112_01_Rab13_CCCP_Vector.RAW Raw
CKondapalli_131112_02_Rab13_CCCP_PINK1WT.RAW Raw
CKondapalli_131112_03_Rab13_CCCP_PINK1KI.RAW Raw
CKondapalli_131112_04_Rab13_-CCCP_Vector.RAW Raw
CKondapalli_131112_05_Rab13_-CCCP_PINK1WT.RAW Raw
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Publications

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 Parkin E3 ligase activity. Here, we have employed quantitative phosphoproteomics to search for novel PINK1-dependent phosphorylation targets in HEK (human embryonic kidney) 293 cells stimulated by mitochondria  ...[more]