SVIL encodes supervillin, a 205-kDa F-actin binding protein that serves as a critical link between the actin cytoskeleton and plasma membranes 1. The protein exhibits a bipartite structure with three nuclear localization signals in the N-terminus and three actin-binding sequences in the C-terminus that share homology with villin 1. SVIL functions in cytoskeletal regulation and cell division, with roles in focal adhesion modulation and cytokinesis. In disease contexts, SVIL demonstrates complex relationships with cancer progression. In bladder cancer, SVIL expression is paradoxically lower in tumor tissue compared to normal tissue, yet high SVIL expression within tumors correlates with poor prognosis 2. SVIL participates in inflammatory responses by mediating LPS-induced cytokine production (IL-6, IL-1β, TNF-α) through TLR4/NF-κB and ERK1/2 pathways in macrophages 3. In hematopoiesis, SVIL expression is regulated by serine metabolism and H3K9 methylation, with downregulation impairing megakaryocyte differentiation and contributing to thrombocytopenia in multiple myeloma 4. Recent genetic studies identify SVIL as a novel hypertrophic cardiomyopathy disease gene, with rare truncating variants conferring approximately tenfold increased HCM risk 5. SVIL also interacts with mutant p53 to recruit chr10 modifiers, promoting gliomagenesis through epitranscriptomic dysregulation 6.