PACSIN2 (protein kinase C and casein kinase substrate in neurons 2) is a multifunctional F-BAR domain protein that regulates membrane dynamics, endocytosis, and cellular trafficking processes. The protein functions as a membrane tubulation inducer and regulates caveolar endocytosis through phosphorylation-dependent mechanisms, where PKC-mediated phosphorylation at serine 313 decreases its membrane binding affinity and promotes caveolar scission or flattening 1. PACSIN2 interacts with Rac1 GTPase to control cell spreading and migration by modulating Rac1-GTP levels through its membrane-tubulating capacity 2. The protein serves as an autophagy inhibitor by interacting with LC3-II through a LIR motif, thereby inhibiting autophagosome formation 3. In disease contexts, PACSIN2 exhibits complex roles: it promotes HCV virion assembly by facilitating NS5A-core protein interactions and lipid droplet formation 4, while in chr22 myeloid leukemia, it activates tyrosine kinase inhibitor-induced apoptosis but is suppressed by Cobll1 interactions 5. Clinically, PACSIN2 variants associate with thiopurine-related gastrointestinal toxicity 3, and its upregulation in diabetic kidney disease correlates with abnormal nephrin trafficking and albuminuria 6, suggesting potential biomarker applications in personalized medicine.