Inverted formin-2 (INF2)

Inverted formin-2 (INF2) is a unique formin-family protein characterized by its abilities to both polymerize and sever actin filaments, thereby regulating cytoskeletal organization. It contains FH1–FH2 domains for actin polymerization and a C-terminal WH2-like domain for filament severing and autoinhibition control. INF2 exists as two splice isoforms: CAAX (prenylated, targeting the endoplasmic reticulum and involved in mitochondrial fission) and non-CAAX (associated with actin networks and Golgi maintenance). It localizes to focal adhesions, dorsal stress fibers, and lamellipodia, where it modulates integrin-mediated adhesion and extracellular matrix organization—processes essential for cell migration, wound healing, and morphogenesis. In podocytes, INF2 antagonizes Rho/mDia signaling, playing a key role in maintaining actin dynamics and proper slit diaphragm protein trafficking. Mutations in the INF2 gene are among the most frequent genetic causes of familial FSGS, a type of kidney disease linked to defects in the glomerular filtration barrier and actin cytoskeleton. No drugs currently target INF2 directly, but its role as an essential cytoskeletal regulator and its disease linkage make it a focus of biomedical research[1][2][3][4].

Other names

Inverted formin 2INF2C14orf151C14orf173MGC13251HBEBP2-binding protein CCMTDIEFSGS5pp9484inverted formin-2HBEAG-binding protein 2 binding protein Cinverted forminFH2 and WH2 domain containing

Not applicable; INF2 is not the target of approved drugs. Its molecular actions include actin polymerization, filament severing, interaction with diaphanous-related formins, and modulation of cytoskeleton organization[1][2][3].