FUS (fused in sarcoma) is a multifunctional RNA-binding protein that plays critical roles in cellular homeostasis and disease pathogenesis. The protein undergoes liquid-liquid phase separation (LLPS) to form membraneless organelles essential for various cellular processes 1. FUS is crucial for DNA repair initiation, where its LLPS activity is necessary for recruiting DNA damage response factors including KU80, NBS1, and 53BP1 to damage sites 2. In healthy neurons, FUS maintains axonal and synaptic function through regulation of mRNA localization, transport, and local translation 3. The protein's nuclear localization is regulated by its import receptor Transportin and arginine methylation, which also suppress pathological phase separation 4. Mutations in FUS cause familial amyotrophic lateral sclerosis (ALS6), characterized by early onset (average 35.2 years) and aggressive progression 5. These mutations disrupt nuclear import, leading to cytoplasmic accumulation and formation of pathological aggregates 6. ALS-associated FUS mutations also alter stress granule composition and dynamics, creating more unstructured, AU-rich transcriptomes that may contribute to neurodegeneration 7. Therapeutically, antisense oligonucleotide-mediated FUS silencing shows promise in reducing protein aggregates and delaying motor neuron degeneration 8.