Federico Diez

TL;DR: The results implicate LRRK2 in primary ciliogenesis and suggest that Rab-mediated protein transport and/or signaling defects at cilia may contribute to L RRK2-dependent pathologies.

TL;DR: It is shown that L RRK2 kinase interferes with primary cilia formation in cultured cells, human LRRK2 G2019S iPS cells and in the cortex of LRRk2 R1441C mice, revealing a molecular pathway for regulating cilia function that likely contributes to Parkinson’s disease-specific pathology.

TL;DR: The MJFF-pRAB10 antibodies can be deployed to assess enhanced Rab10 phosphorylation resulting from pathogenic (R1441C/G or G2019S) LRRK2 knock-in mutations as well as the impact of L RRK2 inhibitor treatment.

TL;DR: These experiments show that LRRK2 generated-phosphoRab10 dramatically redistributes a significant fraction of Myosin Va and RILPL2 to the mother centriole in a manner that likely interferes with Myos in Va’s role in ciliogenesis.

TL;DR: It is shown that LRRK2 generated phosphoRab10 dramatically redistributes Myosin Va-RILPL2 complexes to the mother centriole, which may sequester Myos in Va and RILPL 2 in a manner that blocks their normal roles in ciliogenesis.