This paper reviews two recent studies: one identifying FAM171A2 as a receptor mediating cell-to-cell propagation of misfolded α‑synuclein, and another showing that variable positioning of α‑synuclein terminal regions influences pathogenicity and spread, suggesting that blocking the receptor or…

By pointing to a potentially druggable receptor (FAM171A2) and to structural epitope-targeting strategies that could reduce α‑synuclein spread, the work provides concrete, translatable therapeutic leads for slowing Parkinson’s disease progression.

Knowledge demonstrating the involvement of protein misfolding propagation mechanisms in the progression of Parkinson's disease opens up new therapeutic prospects. This article illustrates this possibility through two recent major publications. The first study focuses on a new receptor (FAM171A2) for abnormally folded α-synuclein protein, which could be blocked to limit the propagation of the pathological protein from cell to cell. The second study highlights that the unstructured ends of this protein have variable positions that may influence its pathogenicity and ability to spread. Modifying this positioning through the action of a substance, such as an antibody, could be an approach to slowing the progression of the disease.