Maxime Teixeira

Phosphorylation and lipid droplets drive the irreversible phase transition of α-Synuclein in living cells

This study uses an optogenetic system to show that phosphorylation and lipid droplets drive the irreversible phase transition of α-synuclein in cells, leading to neurotoxic aggregates linked to Parkinson's disease.

WDR44 drives de novo α-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson's Disease

This study identifies WDR44 as a driver of de novo α-synuclein aggregation at the lysosomal membrane, linking early aggregation events to neuronal dysfunction in Parkinson's Disease.

Recapitulating Parkinson's pathology in human iPSC dopaminergic neurons reveals new mechanistic insights into Lewy body formation and heterogeneity.

This study uses human iPSC-derived dopaminergic neurons to model Parkinson's Lewy body pathology without genetic modification, revealing mechanisms of aSyn aggregation and morphological diversity.

The combination of optogenetic-induced protein aggregation and proximity biotinylation assays strongly implicates endolysosomal proteins in the early stages of α-synuclein aggregation

This paper introduces UltraID-LIPA, a platform combining optogenetic-induced protein aggregation and proximity biotinylation to identify α-synuclein-interacting proteins, revealing endolysosomal proteins' role in early aggregation.