ALS-linked mutations in the low-complexity structural domains of FUS, hnRNPA2B1, EWS, TAF15, MATR3, and TIA1 lead to increased local concentrations of these proteins, enhancing amyloid interactions and forming pathological aggregations of non-functional oligomers and protofibrils, causing difficulty in degrading both autophagy and ubiquitination pathways, which in turn damages neurons [137, 149, 154]. This evidence concerns the gene FUS and amyotrophic lateral sclerosis.