Researchers at Weill Cornell Medicine have uncovered how a key Parkinson’s protein called LRRK2 shifts between inactive and active forms, revealing the structural changes that enable certain mutations to push the protein into an overactive state. Mutations that cause LRRK2 to become abnormally active are among the most common genetic causes of Parkinson’s disease. Even without these mutations, some people with Parkinson’s disease have elevated LRRK2 activity.
Understanding exactly how LRRK2 becomes overactive has become increasingly important because it is one of the leading targets for developing treatments that could slow Parkinson’s disease.
Using electron microscopy and biochemistry, the team captured the structure of LRRK2 in different states, enabling them to elucidate how the protein toggles between active and inactive forms. The findings, published in Cell, point toward a new generation of targeted therapies.
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