Over-expression of L166P-DJ-1 had no effect on ERK1/2 or MEK1/2 phosphorylation, or on the expression of PP2A, even in COS-7
Maraviroc where it is not completely degraded. The L166P mutation of DJ-1 has been reported to be responsible for the onset of familial PD, PARK7 [23]. L166 is located at the middle of α-helix 8 (α
cool and the mutation from leucine to proline appears to cause a break in the α-helix. This results in abrogation of dimer formation, making the protein unstable and more likely to be degraded. In addition, the localization of DJ-1 will be changed by the mutation. Wild-type DJ-1 is localized in the
cytoplasm and nucleus [1] and [4]. The L166P mutated DJ-1 is still present in the nucleus, with any cytoplasmic staining appearing to be mostly colocalized with mitochondria [23]. Proper localization is thought to be necessary for DJ-1 to exert its functions. The partial degradation and loss of cytoplasmic activity are thought to be pathogenic and may be the cause of L166P DJ-1 losing the effect on the ERK1/2 signaling pathway.
