Formin-binding protein 1 (FNBP1)

Formin-binding protein 1 (FNBP1; also known as FBP17) is a scaffolding protein that belongs to the F-BAR (FCH-Bin/Amphiphysin/Rvs) domain family, characterized by its ability to bind curved membranes and regulate actin cytoskeleton dynamics[1][5]. FNBP1 contains several functional domains, including an N-terminal FCH domain, coiled-coil domains, a proline-rich motif, a Rho family protein-binding domain, and a C-terminal SH3 domain[1][5][6]. It participates in membrane tubulation, endocytosis, and the assembly of actin-rich cell protrusions (e.g., filopodia, pseudopodia), partly by recruiting N-WASP to activate Arp2/3-mediated actin polymerization[5]. FNBP1 interacts with proteins such as dynamin, tankyrase, and sorting nexin 2, and is considered integral to the migration and invasion capacities of aggressive tumor cells[2][3][5]. Its expression and function are context-dependent, influencing tumor prognosis and immune cell infiltration in several cancer types[2]. No direct pharmacological modulators are currently known.

Other names

FBP17KIAA0554hFBP17Formin-binding protein 17