Phospholipid Binding: FERM Domain
The FERM domain of mouse Radixin bound to Ins(1,4,5)P3 (red).
Domain Binding and Function
Previously known as the B4.1 (band 4.1) homology and ERM domain, the FERM domain is named for the four proteins in which this domain was originally described: F for Band 4.1, E for Ezrin, R for Radixin, M for Moesin. The FERM domain is approximately 150 amino acids in length and is found in a number of cytoskeletal-associated proteins that are found at the interface between the plasma membrane and the cytoskeleton. The FERM domain is responsible for PIP2 regulated membrane binding of ERM (Ezrin/Radixin/Moesin) proteins that play a role in formation of membraneassociated cytoskeleton by linking actin filaments to adhesion proteins. The structure of the Radixin FERM domain bound to IP3 has been solved, and surprisingly, phosphoinositide binding is not mediated by the PH-fold subdomain of FERM, but occurs at a cleft between two subdomains on a relatively flat face of the module. The FERM domain is also postulated to bind to adhesion proteins, in a PIP2 -regulated fashion, providing a link between cyctoskeletal signals and membrane dynamics.
Structure Reference
- Hamada, K. et al. (2000) EMBO J. 19(17), 4449–4462.
Examples of Domain Proteins
Binding Examples
| FERM Domain Proteins | Binding Partners |
|---|---|
| Radixin | IP3, PI(4,5)P2 |
| ERM | PI(4,5)P2 |
