Cofilin-1 (CFL1)

Cofilin-1 is a small, highly conserved, non-muscle actin-binding protein that is a central regulator of actin filament dynamics. It severs and depolymerizes filamentous (F-) actin and also inhibits the polymerization of monomeric (G-) actin, an activity modulated by its phosphorylation at serine-3 by LIM kinases. Cofilin-1 is involved in controlling cell shape, motility, division, nuclear actin transport, and transcriptional regulation. Its activity is essential for processes such as cytokinesis, migration, and neuronal development. Dysregulated cofilin-1 function has been implicated in cancer metastasis, neurodegenerative disorders, and other diseases involving aberrant cytoskeletal remodeling. As a result, it is considered a potential, though challenging, therapeutic target because systemic inhibition may disrupt fundamental cell functions[1][2][3][4][5][8].

Other names

Cofilin 1CFL1CFLp1818 kDa phosphoproteinCofilinNon-muscle isoform cofilinHEL-S-15Epididymis secretory protein Li 15

Drugs or tool compounds affecting CFL1 act by modulating actin filament turnover through direct inhibition or activation (via phosphorylation/serine-3) or via upstream kinase inhibition (e.g., LIM kinase) Compounds influencing the actin cytoskeleton, migration, or invasion may indirectly affect CFL1 function