Ezrin/radixin/moesin

FERM 4.1/ezrin/radixin/moesin domain Binding to cytoplasmic regions of transmembrane proteins 

PERM PIP2 Band 4.1 protein ezrin, radixin, moesin (ERM)  

FERM FERM-domain (four-point-one ezrin, radixin, moesin) 

Serine/threonine protein phosphatases and ezrin/radixin/moesin proteins 

Poppe D, Tiede 1, Fritz G et al. Azathioprine suppresses ezrin-radixin-moesin-dependent T-cell-APC conjugation through inhibition of Vav guanosine exchange activity on Rac proteins. JImmunol 2006 176 640-651. 

Bretscher, A. 1999. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr. Opin. Cell Biol 11 109-116. 

Tsukita, S. and Yonemura, S. (1999). Cortical actin organization Lessons from ERM (ezrin/radixin/moesin) proteins./. Biol. Chem. 274, 34507-34510. 

Members of the PSD-95 family of proteins have been shown to bind in vitro to band 4.1, an actin/spectrin-binding protein (Lue et al., 1994, 1996 Marfatia et al., 1996). Such an interaction has the potential to link NMDA receptors indirectly to F-actin, which is the predominant cytoskeleton in dendritic spines. Whether band 4.1 or other members of the ezrin-radixin-moesin (ERM) family of actin-binding proteins play a role in postsynaptic anchoring of NMDA receptors and PSD-95 is unknown. 

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