Mutations in the C-terminal domains of FUS and TDP-43 have both been linked to ALS[6],[37].Interestingly, whereas some ALS-linked mutations in TDP-43 can increase stability,aggregation, cytoplasmic accumulation, and toxicity in yeast, mammalian cells, andanimal models [15],[16],[78],[80],[97], the mechanisms by which FUS mutations contribute todisease appear to be distinct. Here, FUS is linked to amyotrophic lateral sclerosis.