| First Author | Hayashi T | Year | 2009 |
| Journal | Biochem Biophys Res Commun | Volume | 390 |
| Issue | 3 | Pages | 667-72 |
| PubMed ID | 19822128 | Mgi Jnum | J:212799 |
| Mgi Id | MGI:5582165 | Doi | 10.1016/j.bbrc.2009.10.025 |
| Citation | Hayashi T, et al. (2009) DJ-1 binds to mitochondrial complex I and maintains its activity. Biochem Biophys Res Commun 390(3):667-72 |
| abstractText | 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. |
