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

Biochem Biophys Res Commun. 2009 Dec 18;390(3):667-72. doi: 10.1016/j.bbrc.2009.10.025. Epub 2009 Oct 12.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Electron Transport Complex I / metabolism*
  • Electron Transport Complex IV / genetics
  • Electron Transport Complex IV / metabolism*
  • Gene Knockdown Techniques
  • Humans
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Mice
  • Oncogene Proteins / genetics
  • Oncogene Proteins / metabolism*
  • Parkinson Disease / enzymology*
  • Protein Binding
  • Protein Deglycase DJ-1


  • Intracellular Signaling Peptides and Proteins
  • Oncogene Proteins
  • Electron Transport Complex IV
  • NDUFA4 protein, human
  • PARK7 protein, human
  • Protein Deglycase DJ-1
  • Electron Transport Complex I