Supervillin (SVIL)

Supervillin (SVIL) is a large, bipartite protein containing both nuclear localization signals and multiple actin-binding sequences homologous to gelsolin family members[1]. It facilitates tight association between actin filaments and the membrane, promoting cellular processes such as spreading, migration, and focal adhesion turnover[1][2]. SVIL attracts actin and cytoskeletal proteins into specialized structures at the plasma membrane and in the nucleus[1]. In cancer, SVIL supports tumor progression by regulating cell survival (notably lowering p53), migration, invasion, and angiogenesis, particularly through vasculogenic mimicry mechanisms and the VEGF/p38 signaling axis[2]. In muscle, supervillin participates in myofibril integrity by physically coupling the sarcolemma to myofibrillar proteins; loss-of-function mutations can result in myopathy[5]. SVIL interacts with androgen receptor and several cytoskeletal elements, suggesting a broad role in cell signaling and structural regulation[1][6][4].

Other names

Archvillinp205p250membrane-associated F-actin binding protein p205MFM10supervillinarchvillincostameric protein SV2

Not applicable for direct drug targeting (no known drugs). Mechanistically, therapeutic investigation would focus on blocking SVIL-mediated actin recruitment, angiogenesis (VEGF/p38 axis), or cytoskeletal remodeling.