Ever wondered how Parkinson’s disease spreads within the brain? A key culprit is the buildup and movement 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: This gene appears to play a crucial role in allowing α-syn fibrils to enter brain cells. Think of it like a receptor that the fibrils latch onto.
• More FAM171A2, more trouble: Higher levels of FAM171A2 mean more α-syn fibrils can get inside neurons, worsening the disease’s spread and toxic effects.
• Less FAM171A2, less damage: When researchers reduced FAM171A2 in neurons, they saw a protective effect against α-syn damage.
• A sticky situation: A specific part of FAM171A2 interacts with a part of the α-syn fibril through electrical attraction, and it’s over 1000 times more likely to bind to the harmful fibrils than the normal protein. This suggests a highly specific targeting mechanism.
• A potential blocker: Scientists have identified a drug called bemcentinib that can disrupt the interaction between FAM171A2 and α-syn fibrils. This has been shown to be effective in cells and even in mice.

This discovery of FAM171A2’s role is a big step forward! It suggests that blocking this “doorway” could be a new avenue for Parkinson’s treatment, potentially slowing or even stopping the progression of the disease. Further research is needed, but this is a promising development for future therapies.