FUS and amyotrophic lateral sclerosis: In ALS patients, FUS mutations (such as R521C and R518G) can still bind to PRMT1 and be methylated, but mutant FUS is more likely to form cytoplasmic inclusions and detain PRMT1 in stress granules, resulting in the loss of its nuclear function, which further aggravates the cytoplasmic aggregation and neurotoxicity of FUS [179].