Supervillin is a protein that in humans is encoded by the SVIL gene. This gene encodes a bipartite protein with distinct amino- and carboxy-terminal domains. The amino-terminus contains nuclear localization signals and the carboxy-terminus contains numerous consecutive sequences with extensive similarity to proteins in the gelsolin family of actin-binding proteins, which cap, nucleate, and/or sever actin filaments. The gene product is tightly associated with both actin filaments and plasma membranes, suggesting a role as a high-affinity link between the actin cytoskeleton and the membrane. The encoded protein appears to aid in both myosin II assembly during cell spreading and disassembly of focal adhesions. Two transcript variants encoding different isoforms of supervillin have been described. [provided by RefSeq].
Forms a high-affinity link between the actin cytoskeleton and the membrane. Isoform 1 (archvillin) is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. Isoform 2 may be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adehesions involves binding to TRIP6 (By similarity).