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

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 s...

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Published in:Biochemical and biophysical research communications 2009-12, Vol.390 (3), p.667-672
Main Authors: Hayashi, Takuya, Ishimori, Chikako, Takahashi-Niki, Kazuko, Taira, Takahiro, Kim, Yun-chul, Maita, Hiroshi, Maita, Chinatsu, Ariga, Hiroyoshi, Iguchi-Ariga, Sanae M.M.
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Language:English
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2009.10.025