We perform extensive studies of the trafficking and processing of alpha synuclein (a-Syn), a protein critically implicated in the pathogenesis of PD and the synucleinopathies. We have discovered that a-Syn normally interacts with brain lipids and affects their content in neurons.  We have further shown that a-Syn associations with brain lipids play an important role in the pathogenic mechanism progressively leading to its missfolding, aggregation and accumulation in Lewy bodies, the prototype pathogenic insults.

Interested to elucidate the normal function of the a-Syn protein in the healthy brain, we found that a-Syn  protein normally act to activate mechanisms of synaptic vesicle recycling following neuronal stimulations, a process that affects among other effects, mechanisms of learning and memory. The function of a-Syn and the toxic properties of its various assemblies is tested in cultured neurons and in relevant mouse models.