Allison Citro

TL;DR: It is shown that TDP-43 can be induced to form inclusions in cell culture and that most T DP-43 inclusions co-localize with SGs, which are cytoplasmic RNA granules that consist of mixed protein - RNA complexes.

TL;DR: expression studies show that tau regulates the distribution of TIA1, and tau accelerates stress granule (SG) formation, and these studies suggest that the pathophysiology of tauopathy requires an intimate interaction with RNA-binding proteins.

TL;DR: Study of RNA-binding proteins and SG biology highlights novel pathways interacting with the pathophysiology of AD, providing potentially new avenues for identifying diseased neurons and potentially novel mechanisms regulating tau biology.

TL;DR: A novel interaction between LRRK2 and the Rho GTPase, Rac1, is demonstrated, which plays a critical role in actin cytoskeleton remodeling necessary for the maintenance of neurite morphology and provides a novel pathway through which L RRK2 might modulate cellular dynamics and contribute to the pathophysiology of Parkinson disease.

TL;DR: RGS2 is identified as a promising target for interfering with neurodegeneration due to LRRK2 mutations in PD patients and found that RGS2 regulates L RRK2 function and neuronal toxicity through its effects on kinase activity and independently of GTPase activity, which reveals a novel mode of action for GAP proteins.