Jean‐Marc Taymans

This study shows that dephosphorylation of LRRK2 at the S910/S935 cluster increases its sensitivity to activation by RAB29, leading to hyperactivation and centrosome cohesion deficits.

This study identifies a regulatory feedback loop between LRRK2 and PP2A phosphatases in Parkinson's disease, showing that LRRK2 phosphorylates PP2A to disrupt its function and contribute to neuronal death.

The paper identifies urinary protein signatures linked to LRRK2 dysfunction in Parkinson's disease using multi-cohort proteomics and machine learning, showing cross-species relevance and potential as pharmacodynamic markers.

This study identifies PAK6 as a modifier of LRRK2 mutations, showing it rescues ciliogenesis defects in G2019S but not R1441C mutations.

Peripheral blood-derived cells can be employed to stratify Parkinson's disease patients most likely to respond to LRRK2-related therapeutics.

The paper identifies two novel LRRK2 variants associated with familial Parkinson's disease and shows they alter phosphorylation and kinase activity.