DJ-1 Is a Redox-Dependent Molecular Chaperone That Inhibits α-Synuclein Aggregate Formation

Shoshana Shendelman, Alan Jonason, Cecile Martinat, Thomas Leete and Asa Abeliovich

PLOS Biology, 2004, vol. 2, issue 11, 1-

Abstract: Parkinson's disease (PD) pathology is characterized by the degeneration of midbrain dopamine neurons (DNs) ultimately leading to a progressive movement disorder in patients. The etiology of DN loss in sporadic PD is unknown, although it is hypothesized that aberrant protein aggregation and cellular oxidative stress may promote DN degeneration. Homozygous mutations in DJ-1 were recently described in two families with autosomal recessive inherited PD (Bonifati et al. 2003). In a companion article (Martinat et al. 2004), we show that mutations in DJ-1 alter the cellular response to oxidative stress and proteasomal inhibition. Here we show that DJ-1 functions as a redox-sensitive molecular chaperone that is activated in an oxidative cytoplasmic environment. We further demonstrate that DJ-1 chaperone activity in vivo extends to α-synuclein, a protein implicated in PD pathogenesis. The interaction of the proteins DJ-1 and α- synuclein described here may be important for understanding the molecular basis of Parkinson's disease.

Date: 2004
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.0020362 (text/html)
https://journals.plos.org/plosbiology/article/file ... 20362&type=printable (application/pdf)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:plo:pbio00:0020362

DOI: 10.1371/journal.pbio.0020362

Access Statistics for this article

More articles in PLOS Biology from Public Library of Science
Bibliographic data for series maintained by plosbiology ().