Stress granules (SGs) are RNA-containing cytoplasmic foci formed in response to 
stress exposure. Since their discovery in 1999, over 120 proteins have been 
described to be localized to these structures (in 154 publications). Most of 
these components are RNA binding proteins (RBPs) or are involved in RNA 
metabolism and translation. SGs have been linked to several pathologies 
including inflammatory diseases, cancer, viral infection, and neurodegenerative 
diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia 
(FTD). In ALS and FTD, the majority of cases have no known etiology and exposure 
to external stress is frequently proposed as a contributor to either disease 
initiation or the rate of disease progression. Of note, both ALS and FTD are 
characterized by pathological inclusions, where some well-known SG markers 
localize with the ALS related proteins TDP-43 and FUS. We propose that TDP-43 
and FUS serve as an interface between genetic susceptibility and environmental 
stress exposure in disease pathogenesis. Here, we will discuss the role of 
TDP-43 and FUS in SG dynamics and how disease-linked mutations affect this 
process.