Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the selective loss of motor neurons, a cell type that is vulnerable to exogenous stress since it cannot be replaced. While two pharmaceutical options exist for ALS, neither truly slows disease nor is an outright cure. Our failing to develop viable therapies is due in part to our incomplete understanding of the fundamental cell biology underlying disease initiation and progression. In recent years, RNA binding proteins and their related proteostasis have emerged as exciting new research areas in this disease. Mutations in one such RNA binding protein TDP-43 are causative for rare familial ALS cases. More striking, however is that TDP-43 is found as a major component of neuronal cytoplasmic inclusions in 97% of all ALS patients (and half of frontotemporal dementia patients) even in the absence of mutation. TDP-43 participates broadly in several aspects of RNA metabolism, including alternative splicing and the integration of environmental stress via stress granule formation. Our current work explores the relevance of TDP-43 loss of function on stress granule dynamics and their role in neuronal vulnerability and degeneration in ALS.
Friday, November 6, 2020
Neurology/Neuroscience Research Seminar
12:00 PM to 1:00 PM
CME credit available, click HERE
Zoom ID: 910 4550 7427 Passcode: 776945