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PINK1-interacting proteins: Proteomic analysis of overexpressed PINK1
Rakovic, Aleksandar; Grünewald, Anne; Voges, Lisa et al.
2011In Parkinsons Dis, 2011, p. 153979
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Abstract :
[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Rakovic, Aleksandar 
Grünewald, Anne   
Voges, Lisa
Hofmann, S
Orolicki, Slobodanka
Lohmann, Katja
Klein, Christine
 These authors have contributed equally to this work.
External co-authors :
yes
Language :
English
Title :
PINK1-interacting proteins: Proteomic analysis of overexpressed PINK1
Publication date :
2011
Journal title :
Parkinsons Dis
Volume :
2011
Pages :
153979
Peer reviewed :
Peer reviewed
Available on ORBilu :
since 12 February 2016

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