 ADF Domain | |
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| Class:Cytoskeletal modulation | |
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Structure:
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Domain binding and function:
The Actin-Depolymerizing Factor (ADF) homology domain or ADF domain is a 130-170 amino acid domain, 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 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 as Drebrin/Adp1 class proteins bind only filamentous actin, while Twinfilins bind only monomeric Actin.
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Examples of Proteins:
| ADF domain protein |
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Binding partner |
| ADF/Cofilin |  |
Filamentous and monomeric actin |
| Drebrin | |
Filamentous actin |
| Twinfilins | |
Monomeric actin |
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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