Crosstalk Between Ubiquitination and Acetylation in the Parkinson's Disease

Parkinson's disease (PD) is amongst the most common neurodegenerative diseases (NDD) in elders. It involves a gradual degeneration of the dopamine-producing neurons and is a main neuropathological characteristic of PD. The post-translational modifications of the proteins tend to crosstalk between one another which might play a significant role in the etiology of Parkinson's disease (PD). Lysine residues on proteins undergo post-translational modifications (PTM) like acetylation and ubiquitination, and these post-translational modifications drive vital cellular functions like transcriptional regulation, autophagy, and in the clearing of the misfolded proteins aggregates by the ubiquitin-proteasome system (UPS) and thus plays a vital role in the degradation of such toxic protein aggregates and also the metabolites toxins present in cells, where some deviation in UPS is generally reported to involve in the Parkinson's Disease (PD). Also, the addition of the acetyl group in lysine and removal of the acetyl group of several proteins, including some proteins like histones and non-histone, might be tightly linked with Parkinson's Disease etiology. But crosstalk between these two PTMs is poorly understood. So, in our review, we will discuss the role of crosstalk between acetylation and ubiquitination in the pathogenesis of PD.