Proteostasis is regulated by ubiquitination, a post-translational signal inducing targeted degradation of unfavorable proteins. In Parkinson’s Disease (PD), a number of ubiquitin pathways can be dysregulated by disease-related mutations, thus contributing to disease pathology. To further understand the effect of dysregulated ubiquitination in PD, it is necessary to understand ubiquitin signaling at a molecular level. Specifically, the work presented here in will determine the effect of post-translational regulation of parkin, a protein that plays a critical role mitophagy, and characterize the biochemical activity of NAB2, a small molecule known to rescue α-synuclein toxicity in a ubiquitin ligasedependent manner. Together, these experiments will provide a biochemical understanding of regulatory mechanisms in PD-related ubiquitin pathways.