PINK1 points Parkin to mitochondria.
For decades, it has been presumed that mitochondrial dysfunction, in the form of impaired complex I activity, may contribute to the cause of Parkinson disease (PD). ( 1)  The discovery that several gene mutations cause familial forms of PD ( 1)  has led to a renewed enthusiasm for the mitochondrial hypothesis of PD, but this time from a quite distinct and, perhaps, more realistic angle. Among these genes, those that code for PTEN-induced kinase-1 (PINK1) ( 2)  and for the E3-ubiquitin ligase Parkin ( 3)  did attract major interest from mitochondriologists, in part, because both proteins interact with each other and apparently function, genetically, within the same molecular pathway to modulate mitochondrial dynamics in Drosophila. ( 4-6).
Vives-Bauza
Cristofol
C
Department of Neurology, Columbia University, New York, NY USA.
Przedborski
Serge
S
D000818:Animals; D001343:Autophagy; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D010300:Parkinson Disease / Q000201:enzymology / Q000473:pathology; D011494:Protein Kinases / Q000378:metabolism*; D015398:Signal Transduction; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination; D050995:Voltage-Dependent Anion Channel 1 / Q000378:metabolism; D000099202:PTEN-Induced Putative Kinase
D011494:Protein Kinases; D044767:Ubiquitin-Protein Ligases; D050995:Voltage-Dependent Anion Channel 1; D000099202:PTEN-Induced Putative Kinase; C111567:parkin protein