VAPA (VAMP associated protein A) is an endoplasmic reticulum (ER)-anchored protein that plays critical roles in membrane contact site formation and lipid transport. VAPA mediates the formation of contact sites between the ER and multiple organelles through interactions with FFAT motif-containing proteins 1. The protein enables cholesterol transport from the ER to endosomes via interaction with STARD3 and participates in neosynthesized protein export through WDR44 binding 23. VAPA serves as a crucial component in ER-lysosome contacts that enable cholesterol sensing by mTORC1, with OSBP-VAPA complexes delivering cholesterol to lysosomes for growth signaling activation 4. The protein's intrinsically disordered regions (IDRs) provide conformational flexibility, allowing adaptation to various membrane contact sites including ER-mitochondria and ER-Golgi contacts 1. During cell motility, VAPA is essential for maintaining plasma membrane phosphoinositide levels, focal adhesion dynamics, and anchoring ventral ER-plasma membrane contact sites 5. VAPA also facilitates viral replication processes, with respiratory syncytial virus exploiting VAPA-mediated cholesterol transport to promote infection 6. Additionally, VAPA-enriched extracellular vesicles contribute to hepatocellular carcinoma bone metastasis by activating osteoclasts 7.