Other: ADF Domain
The ADF domain in yeast cofilin.
Domain Binding and Function
The Actin-Depolymerizing Factor (ADF) homology domain (ADF domain) is a 130–170 amino acid sequence, first identified in the ADF family of proteins, that is associated with proteins involved in F-actin severing. The domain functions as an actin-binding module present in an extensive family of proteins, including ADF/Cofilin, the Twinfilins and Drebrin/Adp1. This evolutionarily primitive domain pre-dates the divergence of fungi and animals and is found in all eukaryotic organisms. The ADF-containing proteins ADF, Cofilin, Depactin and Actophorin bind to monomeric and filamentous actin and that act to sever Actin filaments. This creates more plus (barbed) and minus (pointed) ends allowing faster Actin turnover and results in the observation that these proteins both rapidly depolymerize filamentous Actin in vitro, as well as increase the rate of F-actin polymerization. Certain ADF-containing proteins appear to have developed more specialized functions. For example, the Drebrin/Adp1 class proteins bind only filamentous actin, while Twinfilins bind only monomeric Actin.
- Fedorov, A.A. et al. (1997) Nat. Struct. Biol. 4(5), 366–369.
Examples of Domain Proteins
|ADF Domain Protein||Binding Partners|
|ADF/Cofilin||Filamentous and monomeric actin|