Recent publications suggest that the Parkinson's disease- (PD-) related 
PINK1/Parkin pathway promotes elimination of dysfunctional mitochondria by 
autophagy. We used tandem affinity purification (TAP), SDS-PAGE, and mass 
spectrometry as a first step towards identification of possible substrates for 
PINK1. The cellular abundance of selected identified interactors was 
investigated by Western blotting. Furthermore, one candidate gene was sequenced 
in 46 patients with atypical PD. In addition to two known binding partners 
(HSP90, CDC37), 12 proteins were identified using the TAP assay; four of which 
are mitochondrially localized (GRP75, HSP60, LRPPRC, and TUFM). Western blot 
analysis showed no differences in cellular abundance of these proteins comparing 
PINK1 mutant and control fibroblasts. When sequencing LRPPRC, four exonic 
synonymous changes and 20 polymorphisms in noncoding regions were detected. Our 
study provides a list of putative PINK1 binding partners, confirming previously 
described interactions, but also introducing novel mitochondrial proteins as 
potential components of the PINK1/Parkin mitophagy pathway.