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FERM domain

Class: Phospholipid Binding

Brief description: The FERM domain is about 300 amino acids long and is found in the N-terminal region of the ezrin/radixin/moesin (FRM) family of proteins. They function as cross-linkers between plasma membranes and actin filaments and have been found in eukaryotic cells. Localisation of FERM poteins in cell-surface structures and cell adhesion sites where actin filaments associate with plasma membrane have been revealed. They have also been found in various other proteins such as tyrosine phosphateses. They have been shown to bind PtdIns(4,5)P2 in vitro.

Structure:

structure Crystal structure of the radixin FERM domain shows that the domain is composed of three subdomains (A, B and C) that are arranged like a clover-leaf. C-subdomain is similar to PH domain. In all the complexes obtained under various conditions, IP3 binding site is located in the basic cleft between subdomains A and C. This positivley charged cleft is formed by C-terminal helix of subdomain C and protruding loops of subdomain A. Due to the absence of flanking aromatic/hydrophobic residues, FERM domains in not expected to penetrate significantly into IP3 containing membranes. A small conformational change appears to occur on IP3 binding site, but an allosteric mechanism can not be supported.

Subcellular Localization:

The FERM domain has been shown to be localized to membranes containing PtdIns(4,5)P2 in vitro. ERM proteins are kept in a dormant conformation in the cytoplasm by the interdomain interaction between the FERM domain and the C-terminal domain.

Get the sequences in a Swiss-Prot/Uniprot pattern and Tab-delimited format.

Browse through the structures available.

Relevant Literature

1. Tsukita, S., Yonemura, S. and Tsukita, S. (1997) ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem Sci, 22, 53-58.

2. Hamada, K., Shimizu, T., Matsui, T., Tsukita, S. and Hakoshima, T. (2000) Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. Embo J, 19, 4449-4462.

3. Hirao, M., Sato, N., Kondo, T., Yonemura, S., Monden, M., Sasaki, T., Takai, Y., Tsukita, S. and Tsukita, S. (1996) Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol, 135, 37-51.

4. Lee, H.S., Bellin, R.M., Walker, D.L., Patel, B., Powers, P., Liu, H., Garcia-Alvarez, B., de Pereda, J.M., Liddington, R.C., Volkmann, N. et al. (2004) Characterization of an actin-binding site within the talin FERM domain. J Mol Biol, 343, 771-784.