ArticlebioRxiv : the preprint server for biology2025
mGluR4-Npdc1 complex mediates α-synuclein fibril-induced neurodegeneration.
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Fibrils of misfolded α-synuclein (α-syn) accumulate in Parkinson's disease and other synucleinopathies, spreading between cells to template further misfolding and drive neurodegeneration. α-syn fibril entry into healthy neurons is recognized as a key step in the disease process but remains ill-defined mechanistically. Here, we comprehensively assessed the membrane proteome for binding of α-syn fibrils. Expression cloning identified mGluR4 and Npdc1 as plasma membrane proteins expressed by substantia nigra neurons capable of supporting high affinity α-syn fibril binding. Moreover, mGluR4 and Npdc1 cellular signaling functions were titrated by the presence of extracellular fibrillary α-syn. While striatal α-syn fibril injection led to nigral dopamine neuron loss in wild type mice, deletion of either
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