Flightless I actin-binding protein (FLII)

Flightless I actin-binding protein (FLII) is a member of the gelsolin family of actin-remodeling proteins that regulates cytoskeletal organization by binding to both G-actin and F-actin, capping the barbed ends, and inhibiting actin polymerization, yet lacking actin-severing activity[2][1]. FLII contains six gelsolin-like domains and a unique N-terminal leucine-rich repeat (LRR) domain, enabling diverse protein-protein interactions[2][1]. It plays key roles in actin-dependent processes such as cell migration, extension formation, adhesion, and extracellular matrix remodeling—promoting collagen compaction through interaction with nonmuscle myosin IIA[1]. In nuclei, FLII contributes to chromatin remodeling and transcriptional regulation by interacting with the SWI/SNF complex and estrogen receptor alpha[2]. FLII is essential for normal wound healing, embryogenesis, and muscle structure, with mutations linked to defects such as cardiomyopathy via disruption of sarcomeric actin dynamics[3]. There are currently no direct therapeutic drugs targeting FLII, nor is it classified as a canonical therapeutic target such as a receptor, enzyme, or transporter.

Other names

Protein flightless-1 homologFLILFLIFli1MGC39265CMD2JFlightless I actin binding proteinFlightless I homolog