VPS13A is a lipid transport protein that mediates transfer of lipids between organelle membranes at contact sites 1. The protein contains an N-terminal tubular domain with a hydrophobic cavity capable of solubilizing and transporting glycerolipids 1. VPS13A localizes to the ER, mitochondria, and lipid droplets, where it interacts with ER-resident protein VAP-A via its FFAT domain and with mitochondria through its C-terminal domain 2. VPS13A is required for establishing and maintaining ER-mitochondria contact sites that enable lipid transfer, regulates mitochondrial morphology, and negatively controls lipid droplet size and motility 2. The protein is also essential for efficient lysosomal protein degradation and autophagy 3. Mutations in VPS13A cause chorea-acanthocytosis, an autosomal recessive neurodegenerative disorder 4. VPS13A deficiency impairs autophagy in skeletal muscle, resulting in cellular energy depletion, defective myofibril stability, and premature muscle senescence characterized by accumulation of senescence markers and activation of pro-inflammatory pathways 3. The clinical heterogeneity observed in VPS13A disease may reflect additional mutations in genes encoding VPS13A-interacting partners 5. Rapamycin treatment can rescue autophagy and senescence markers, suggesting therapeutic potential 3.