TOR1A encodes torsin-1A, an AAA+ ATPase chaperone protein that plays crucial roles in protein quality control and cellular organization. The protein functions primarily in the endoplasmic reticulum and nuclear envelope, where it assists in protein folding, prevents misfolded protein aggregation, and maintains nuclear envelope integrity 1. TOR1A is particularly important in neuronal function, regulating synaptic vesicle recycling and dopamine neurotransmission through control of dopamine transporter localization 1. The gene exhibits complex inheritance patterns with distinct disease associations. Heterozygous mutations cause DYT1 dystonia, an early-onset generalized dystonia with reduced penetrance and autosomal dominant inheritance 2. Meta-analysis has identified specific TOR1A polymorphisms (rs1182 and rs1801968) associated with focal dystonia and writer's cramp 3. In contrast, biallelic TOR1A variants cause arthrogryposis multiplex congenita 5 (AMC5), a severe neurodevelopmental disorder characterized by congenital contractures, developmental delay, and high mortality 4. The protein's dysfunction contributes to endoplasmic reticulum stress response pathways implicated in dystonia pathogenesis 1, highlighting its critical role in maintaining neuronal proteostasis and proper brain network function.