Fascin actin-bundling protein 1 (FSCN1)

Fascin actin-bundling protein 1 (FSCN1) is a 55 kDa cytoskeletal protein highly conserved in vertebrates, primarily involved in cross-linking F-actin into tight, parallel bundles. Structurally, fascin contains four β-trefoil domains and at least two major actin-binding sites, which enable its actin-bundling function; dimerization is necessary for activity[1][2][3][4]. It organizes actin filaments to form cell structures such as filopodia, microspikes, and invadopodia, essential for cell migration, membrane dynamics, and invasive behavior[1][5]. Overexpression or dysregulation of fascin is strongly implicated in various human cancers, correlating with enhanced tumor cell migration, invasion, metastasis, and poor clinical outcomes[6]. Because of its central role in cancer cell motility and metastasis, fascin is being pursued as a therapeutic target, with several small-molecule inhibitors in development[3][6]. Fascin is also expressed in normal physiological contexts, including neuronal and immune cells, where it regulates cell structure and movement.

Other names

Fascinp55actin-bundling protein fascinfascin-1

Inhibitors bind to actin-binding sites, blocking fascin actin-bundling activity, impeding cancer cell migration and invasion[2][3].