Figure 4From: Oxidation of the cysteine-rich regions of parkin perturbs its E3 ligase activity and contributes to protein aggregationMapping locations of parkin oxidation in comparison to parkin mutations found in PD patients. Parkin (PARK2, UniProt 060260; NCBI AB009973) with 465-aa residues and its various domains indicated [Ubiquitin-like (Ubl), RING I and II, and in-between RING (IBR) domains]. (A) Sulfonated peptides of parkin were identified by either Q-TOF and/or Ion trap MS/MS, and labeled by "─" corresponding to the location of their sequence. Complementary MS analysis demonstrated that the identified cysteine residues in peptide fragments of parkin in the RING and IBR domains (16/22 = 73%) were highly reactive with ROS and formed sulfination/sulfonation derivatives of cysteine. (B), Parkin mutations identified in patients with familial Parkinson's disease (http://www.uniprot.org/uniprot/O60260), revealing high homology with modifications induced by oxidative stress.Back to article page