Suzanne R. Pfeffer

The paper shows that G51D alpha-synuclein mice exhibit loss of primary cilia and neurotrophic signaling in specific brain regions, linking ciliary dysfunction to Parkinson's disease pathology.

This study shows that LRRK2 and GCase regulate BMP release via EVs, with mutant LRRK2 increasing EV-associated BMP and GCase modulating this effect.

This study identifies an allosteric site on PPM1H phosphatase that binds non-phosphorylated Rab8A and Rab10, inhibiting its activity and regulating LRRK2 substrate dephosphorylation.

This paper shows that mutations in LRRK2 and GBA1 impair Hedgehog signaling in the striatum through distinct mechanisms, contributing to Parkinson's disease pathogenesis.

The paper identifies PPM1M as a phosphatase that reverses LRRK2-mediated Rab phosphorylation and links a rare mutation to Parkinson's disease.

The paper shows that LRRK2 kinase inhibitor treatment restores cilia, Hedgehog signaling, neuroprotective factors, and dopamine processes in Parkinson's linked-LRRK2 mutant mice striatum.

This study shows LRRK2 and PINK1 function in parallel neuroprotective pathways affecting ciliogenesis in Parkinson's disease, suggesting shared therapeutic targets.

The paper shows that LRRK2 mutations cause loss of primary cilia and Neurturin in striatal Parvalbumin interneurons, impairing neuroprotective signaling.

The paper shows that loss of primary cilia in specific striatal cell types reduces dopaminergic neuroprotection in Parkinson's disease, linked to impaired Hedgehog signaling.

This study shows that the VPS35[D620N] mutation causes lysosomal dysfunction, activates LRRK2, and promotes the lysosomal association of RILPL1 and TMEM55B through phosphorylation of Rab proteins.