This study investigates the role of acetylated α-tubulin redistribution in Parkinson's disease (PD) pathology, focusing on its relationship with α-synuclein aggregation and Lewy body (LB) formation. Using post-mortem human brain samples from PD patients and controls, the researchers observed a redistribution of acetylated α-tubulin in subcortical regions, particularly in neuronal cell bodies, while its levels decreased in axonal compartments. This redistribution was linked to α-synuclein oligomerization and phosphorylated Ser129 α-synuclein, suggesting a potential role in LB formation. The study also identified threadlike structures resembling tunnelling nanotubes containing α-synuclein oligomers and associated with acetylated α-tubulin-enriched neurons. These findings support the hypothesis that acetylated α-tubulin plays a significant role in PD pathogenesis and LB formation. The study highlights the complex interplay between acetylated α-tubulin and α-synuclein, providing insights into the mechanisms underlying PD progression. The results suggest that acetylated α-tubulin may be involved in the early stages of α-synuclein aggregation and the formation of LBs, and that its redistribution could be a key factor in the disease's progression. The study also underscores the importance of in vivo analysis in understanding the complex pathological processes of PD.This study investigates the role of acetylated α-tubulin redistribution in Parkinson's disease (PD) pathology, focusing on its relationship with α-synuclein aggregation and Lewy body (LB) formation. Using post-mortem human brain samples from PD patients and controls, the researchers observed a redistribution of acetylated α-tubulin in subcortical regions, particularly in neuronal cell bodies, while its levels decreased in axonal compartments. This redistribution was linked to α-synuclein oligomerization and phosphorylated Ser129 α-synuclein, suggesting a potential role in LB formation. The study also identified threadlike structures resembling tunnelling nanotubes containing α-synuclein oligomers and associated with acetylated α-tubulin-enriched neurons. These findings support the hypothesis that acetylated α-tubulin plays a significant role in PD pathogenesis and LB formation. The study highlights the complex interplay between acetylated α-tubulin and α-synuclein, providing insights into the mechanisms underlying PD progression. The results suggest that acetylated α-tubulin may be involved in the early stages of α-synuclein aggregation and the formation of LBs, and that its redistribution could be a key factor in the disease's progression. The study also underscores the importance of in vivo analysis in understanding the complex pathological processes of PD.