To address this, we analyzed the presence of SLP2/PHB aggregates in two well-established ALS mouse models with distinct pathogenic mechanisms: the Sod1G86R transgenic model, which mimics toxic gain-of-function effects of mutant SOD1 and is characterized by mitochondrial stress and oxidative damage [22,23]; and the FusΔNLS knock-in model, which presents a defective nuclear localization signal, leading to cytoplasmic FUS accumulation and downstream TDP-43 pathology [24,25]. The gene discussed is PHB1; the disease is amyotrophic lateral sclerosis.