Ever wonder how Parkinson’s disease spreads within the brain? A key culprit is the build-up of abnormal alpha-synuclein (α-syn) protein clumps, called fibrils. New research has uncovered a fascinating piece of the puzzle: a gene called FAM171A2.

• FAM171A2 acts as a doorway: Think of FAM171A2 as a receptor on the surface of brain cells. This receptor appears to play a significant role in allowing α-syn fibrils to enter the cells.
• More FAM171A2, more trouble: Studies show that higher levels of FAM171A2 lead to increased uptake of these harmful α-syn fibrils, worsening their spread and toxic effects within the brain.
• Less FAM171A2, less damage: Conversely, reducing FAM171A2 levels seems to protect brain cells from the damaging effects of α-syn.
• How it works: The FAM171A2 protein interacts with a specific part of the α-syn fibril, drawing it into the cell. This interaction is highly specific to the fibril form of α-syn, meaning it’s much less likely to bind to the healthy form of the protein.
• A potential treatment target: Researchers have identified a drug called bemcentinib that can block the interaction between FAM171A2 and α-syn fibrils. This exciting discovery suggests that blocking this interaction could be a new avenue for treating Parkinson’s disease.

This research highlights FAM171A2 as a potential therapeutic target for Parkinson’s disease. By blocking its interaction with α-syn fibrils, we may be able to slow or even halt the progression of this debilitating disease. Further research is needed to fully understand the role of FAM171A2 and to develop effective therapies targeting this pathway.