Anti-Supervillin antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Supervillin also known as SVIL is a multifunctional protein with a molecular mass of approximately 205 kDa. It plays a significant role in cytoskeletal dynamics by acting as a scaffolding protein connecting actin filaments. This connection facilitates the modulation of cellular structure and motility. The protein is ubiquitously expressed with high levels found in muscle endothelial and certain epithelial cells. Supervillin has fundamental elements such as multiple ankyrin repeat domains sequences resembling gelsolin and villin headpieces which aid in its multifunctionality.

Biological function summary

Supervillin contributes to the formation and organization of cytoskeletal components. It exists as part of a larger protein complex that regulates actin filament assembly and stabilization. This protein influences cell adhesion migration and possibly axonal growth by providing a structural framework and regulatory interface. Its interaction with myosin II further suggests a role in cellular contraction events adding another layer of complexity to its biological function.

Pathways

Supervillin integrates into important cellular processes such as the regulation of the actin cytoskeleton and cell adhesion pathways. It operates in conjunction with other proteins like integrins contributing to focal adhesion dynamics. Another key pathway involves RhoA signaling where Supervillin participates in modulating cell shape and motility. It collaborates with proteins in the Rho family to control actin filament rearrangements vital for cell movement and tissue architecture.

Associated diseases and disorders

Disruptions in Supervillin function link to muscular dystrophies and certain types of cancer. Altered expression levels can influence the invasive potential of cancer cells and affect tumor progression through interactions with proteins like integrins and other components of adhesion complexes. In muscular disorders the relationship with myosin II highlights a connection to muscle contraction abnormalities contributing to disease pathology. These associations emphasize the importance of Supervillin in maintaining cellular and tissue integrity.