InterPro domain: IPR017904

Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits [ 1 , 2 , 3 ]. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin) [ 4 , 5 ]. The modes of action of ADF/cofilins highly depend on their concentration. When ADF/cofilins are present in low concentrations they prefer to sever the actin filaments and promote the depolymerization of the pointed end of the filament. At high concentrations they can increase the polymerization by nucleating new actin filaments [ 6 ].

1. Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol. 9, 364-70
2. The other side of the coin: functional and structural versatility of ADF/cofilins. Eur. J. Cell Biol. 93, 238-51
3. Biophysics of actin filament severing by cofilin. FEBS Lett. 587, 1215-9
4. The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Mol. Biol. Cell 13, 183-94
5. ADF/cofilin: a functional node in cell biology. Trends Cell Biol. 20, 187-95
6. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol. Cell 24, 13-23