Abstract: Protein aggregation is related to a large number of neurodegenerative disorders. Particularly in some cases, aggregation is induced by hyperphosphorylation of a given protein. This is the case of tau, TAR DNA-binding protein 43 (TDP-43), amyloid-beta peptides (Aβ) and alpha-synuclein (α-syn), which play a key pathogenic role in Alzheimer’s disease (AD), Parkinson’s disease (PD) and amyotrophic lateral sclerosis, among others (Tenreiro et al., 2014; Chiti and Dobson, 2017). In this perspective, we will discuss both the relationship between phosphorylation and amyloid aggregation as well as current and future therapeutic strategies aimed at inhibiting specific kinases involved in the phosphorylation step or inhibiting subsequent protein aggregation. Moreover, we will address novel approaches that are based on chemical-inducing proximity, to recruit the proteasome, the autophagy-lysosome system or specific phosphatases to degrade or dephosphorylate the target proteins. We want to focus our interest on proteolysis-targeting chimeras (PROTACs) systems, which represent one of the newest and most interesting therapeutic approaches that could be applicable to phosphorylation-driven aggregative proteins in the near future (Ciechanover and Kwon, 2015; Esposto and Martic, 2021; Jangampalli et al., 2021; Jiang et al., 2021).