In ALS, mutations in SOD1, TDF43, or FUS1 lead to protein aggregation which in turn starts a sequence of events ultimately culminating in metabolic and cellular failure. As a first step in the sequence of events, aggregated proteins lead to mitochondrial dysfunction causing a drop in ATP levels and concomitantly increasing ROS levels. The loss in membrane potential triggers cytochrome c release leading to the initiation of apoptotic signaling. ROS also drives increased Drp1 association with the mitochondria leading to sustained mitochondrial fission and fragmentation. Due to the drop in ATP levels, cellular functions such as autophagy and proteasomal degradation are affected leading to increased protein aggregates, which trigger ER stress. This leads to further impaired protein quality control, thus feeding back into a vicious cycle. P110, through inhibition of mitochondrial fragmentation, helps restore mitochondrial health, thereby breaking the vicious loop caused by mutated ALS‐related proteins.