Abstract:
:Loss-of-function DJ-1 mutations can cause early-onset Parkinson's disease. The function of DJ-1 is unknown, but an acidic isoform accumulates after oxidative stress, leading to the suggestion that DJ-1 is protective under these conditions. We addressed whether this represents a posttranslational modification at cysteine residues by systematically mutating cysteine residues in human DJ-1. WT or C53A DJ-1 was readily oxidized in cultured cells, generating a pI 5.8 isoform, but an artificial C106A mutant was not. We observed a cysteine-sulfinic acid at C106 in crystalline DJ-1 but no modification of C53 or C46. Oxidation of DJ-1 was promoted by the crystallization procedure. In addition, oxidation-induced mitochondrial relocalization of DJ-1 and protection against cell death were abrogated in C106A but not C53A or C46A. We suggest that DJ-1 protects against neuronal death, and that this is signaled by acidification of the key cysteine residue, C106.
journal_name
Proc Natl Acad Sci U S Aauthors
Canet-Avilés RM,Wilson MA,Miller DW,Ahmad R,McLendon C,Bandyopadhyay S,Baptista MJ,Ringe D,Petsko GA,Cookson MRdoi
10.1073/pnas.0402959101keywords:
subject
Has Abstractpub_date
2004-06-15 00:00:00pages
9103-8issue
24eissn
0027-8424issn
1091-6490pii
0402959101journal_volume
101pub_type
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