Ever wonder how Parkinson’s disease spreads within the brain? A key player is a protein called alpha-synuclein (α-syn), which forms harmful clumps called fibrils. Researchers have been working hard to understand how these fibrils get into brain cells, and a new study has uncovered some exciting clues.

They’ve identified a gene, FAM171A2, that seems to act like a doorway for α-syn fibrils to enter neurons. Think of it like a lock and key: the α-syn fibril is the key, and FAM171A2 is the lock on the neuron’s surface. When they connect, the fibril gets pulled inside.

Here’s a breakdown of the findings:

• FAM171A2 increases risk: Having higher levels of this gene makes it easier for α-syn fibrils to get into neurons, worsening Parkinson’s symptoms.
• Blocking FAM171A2 is protective: When researchers reduced FAM171A2 in neurons, the uptake of α-syn fibrils decreased, offering a potential protective effect against the disease’s progression.
• How the interaction works: The study showed a specific part of FAM171A2 interacts strongly with a part of the α-syn fibril, like a perfect fit. This interaction is incredibly selective for the harmful fibril form of α-syn, making it a promising target.
• A potential new drug? Researchers identified a drug called bemcentinib that can block the interaction between FAM171A2 and α-syn fibrils. This discovery offers a potential new avenue for Parkinson’s treatment, aiming to stop the spread of the disease at its source.

This research represents a significant step forward in understanding how Parkinson’s disease progresses. By identifying FAM171A2 as a key player in the uptake of α-syn fibrils, and finding a potential blocker in bemcentinib, scientists have opened up exciting new possibilities for developing effective therapies for this devastating disease. Further research will be crucial to explore the full potential of these findings and translate them into treatments that can benefit patients.