DJ-1 binds to mitochondrial complex I and maintains its activity

Takuya Hayashi, Chikako Ishimori, Kazuko Takahashi-Niki, Takahiro Taira, Yun-chul Kim, Hiroshi Maita, Chinatsu Maita, Hiroyoshi Ariga, Sanae M M Iguchi-Ariga
Biochemical and Biophysical Research Communications 2009 December 18, 390 (3): 667-72
Parkinson's disease (PD) is caused by neuronal cell death, and oxidative stress and mitochondrial dysfunction are thought to be responsible for onset of PD. DJ-1, a causative gene product of a familial form of Parkinson's disease, PARK7, plays roles in transcriptional regulation and anti-oxidative stress. The possible mitochondrial function of DJ-1 has been proposed, but its exact function remains unclear. In this study, we found that DJ-1 directly bound to NDUFA4 and ND1, nuclear and mitochondrial DNA-encoding subunits of mitochondrial complex I, respectively, and was colocalized with complex I and that complex I activity was reduced in DJ-1-knockdown NIH3T3 and HEK293 cells. These findings suggest that DJ-1 is an integral mitochondrial protein and that DJ-1 plays a role in maintenance of mitochondrial complex I activity.

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