Ezrin/radixin/moesin

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

The bacterium Pseudomonas aeruginosa produces several virulence factors. In particular ExoS has an ADP-ribosylation domain that affects arginine residues. When pleotypic cells are infected with ExoS, the phosphorylation of ezrin/radixin/moesin (ERM) proteins no longer occurs." It happens that ERM proteins are high-afifmity substrates for the ADP-ribosylation domain of ExoS. When the sequence of moesin was... 

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. 

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

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. 

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

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

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

Yonemura, S., Matsui, T., Tsukita, S. and Tsukita, S. (2002). Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins an essential role for polyphosphoinositides in vivo. J. Cell Sci. 115, 2569-2580. Yoshinaga-Ohara, N., Takahashi, A., Uchiyama, T. and Sasada, M. (2002). Spa-tiotemporal regulation of moesin phosphorylation and rear relase by Rho and serine/threonine phsophatase during neutrophil migration. Exp. Cell Res. 278, 112-122. 

Mackay, D.J., Esch, E., Eurthmayr, H., Hall, A. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in penneabUized fibroblasts an essential role for ezrin/radixin/moesin proteins. J. CeU Biol. 138, 927-938 (1997)... 

Hess F, Estrugo D, Fischer A et al (2007) Integrin-linked kinase interacts with caspase-9 and -8 in an adhesion-dependent manner for promoting radiation-induced apoptosis in human leukemia cells. Oncogene 26 1372-1384 Hirao M, Sato N, KondoT etal (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... 

ERM proteins belong to the band 4.1 superfamily, which also includes the tumor suppressor merlin ERM proteins share three highly conserved structural domains. The N-terminal PERM (/our-point one, ezrin, radixin, moesin) domain binds directly or indirectly to membrane proteins, whereas the C-terminal domain binds F-actin, resulting in actin filament rearrangement. ERM proteins therefore act as cross-linkers between cell membrane proteins and the actin cytoskeleton. The N- and C-terminal domains are linked by an a-helical coiled domain that modulates ERM actions ERM proteins are located in the cytoplasm in a dormant state due to inhibitory interactions between their N- and C-domains. They are activated by phosphorylation and/or interactions with phospholipids, whereupon they move to a submembranous location. 

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