Anti- FNBP1

FNBP1 (formin binding protein 1) also known as FBP17,is an F-BAR domain protein that belongs to the formin-binding-protein family. It has a powerful self-polymerizing ability that promotes actin nucleation on membranes. F-BAR domain of FBP17 is capable of self-polymerizing into filaments, which adhere to the flat bilayer sheets and form a spiral protein coat around the tubulated membrane that they then induce. The gene for FNB1 maps to chromosome 9q34 and consists of a C-terminal Src homology 3 domain and an N-terminal region that is homologous to the cell division cycle protein, cdc15, a regulator of the actin cytoskeleton. The assembly of FBP17 is dependent on WASP, and its dissociation by WASP inhibition strongly induces a self-organization of PSTPIP2, another F-BAR protein, at podosomes. Podosomes/invadopodia are highly dynamic adhesive actin-based structures with enrichment of matrix metalloproteases (MMPs) activity formed at the ventral surface of the cell body, which are seen in macrophages, osteoclasts, dendritic cells and some cancer cells. Protein function: May act as a link between RND2 signaling and regulation of the actin cytoskeleton. Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL. [The UniProt Consortium]