Biochem Biophys Res Commun. 2009 Dec 18;390(3):667-72. Epub 2009 Oct 12.

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

Hayashi T, Ishimori C, Takahashi-Niki K, Taira T, Kim YC, Maita H, Maita C, Ariga H, Iguchi-Ariga SM.

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Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan.

Abstract

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.

PMID:: 19822128; [PubMed - indexed for MEDLINE]

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Cited by 7 PubMed Central articles

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Mitochondrial Dysfunction: The Road to Alpha-Synuclein Oligomerization in PD. [Parkinsons Dis. 2011]
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