DJ-1 Is a Redox-Dependent Molecular Chaperone That Inhibits α-Synuclein Aggregate Formation
By S. Shendelman, A. Jonason, C. Martinat, T. Leete, A. Abeliovich. PLoS Biology, 2004
618 citations recorded by the source corpus.
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.
Subfields: Cell Biology, Neurology
View Paper: https://www.semanticscholar.org/paper/6409a456d1e03848916a889a3aae90646e169d69
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Citations in the corpus
- Expanding insights of mitochondrial dysfunction in Parkinson's disease (2006, background): “In addition to cellular response to oxidative damage and apoptosis, DJ1 also functions as a redox sensitive molecular chaperone that is capable of preventing the aggregation of α-synuclein and the neurofilament subunit NF”
- Glyoxalase and Methylglyoxal as Biomarkers for Plant Stress Tolerance (2014, background): “Bacterial and human DJ-1 proteins act as molecular chaperones, interacting with unfolding intermediates, preventing aggregation (Shendelman et al., 2004; Subedi et al., 2011).”