“…Phosphorylation at serine-129 was reported to induce the formation of distinct α-syn strains (14), and phosphorylated exogenous α-syn fibrils could exacerbate pathology and induce neuronal dysfunction in mice (15). A recent report also concluded that p-α-syn enhanced the interaction between αsyn fibrils and its receptors, which meant that p-α-syn could facilitate the spread of α-syn pathologies (16). Overall, the role of p-α-syn is relatively complicated, and further studies Abbreviations: α-syn, α-synuclein; AP, alkaline phosphatase; β-syn, β-synuclein; BCA, bicinchoninic acid; C, C-terminal domain of α-synuclein (residues 96-140); CBS, Coomassie Brilliant Blue staining; ELISA, enzyme-linked immunosorbent assay; h-α-syn, human α-synuclein; m-α-syn, mouse α-synuclein; MS, mass spectrometry; N, N-terminal domain of α-synuclein (N-α-syn, residues 1-60); N, N-terminal domain of α-synuclein; NAC, non-amyloid component, the central domain of α-synuclein (residues 61-95); p, phospho-group; p-α-syn, serine-129site phosphorylated α-synuclein; PD, Parkinson's disease; PFF, preformed fibrils; PLK3, Polo-Like-Kinase 3; pNPP, p-nitrophenyl phosphate; KO, α-syn knockout mice; R, rabbit; SD, standard deviation; SEM, standard error of the mean; TEM, transmission electron microscopy; Tg, Thy1-SNCA transgenic mice; ThT, thioflavin T; Wt, wild-type brood mice.…”