The ERM family of proteins is composed of Ezrin, Radixin, and Moesin. ERM proteins regulate the linkage of cortical actin to membrane-associated proteins in cellular substructures by directly binding to both. Ezrin is the most studied of all ERM proteins and was identified as an 81 kDa substrate protein for receptor tyrosine kinase in A431 carcinoma cell lines (Hunter and Cooper 1981). Subsequently, it was purified as an 80 kDa protein from intestinal microvilli (Bretscher 1983). In an independent study, when an antibody was used against a 75 kDa synthetic peptide derived from cloned human endogenous retrovirus gag-related DNA sequence erv1, a protein named cytovilin was identified (Suni et al. 1984). It was found to be enriched in microvilli (Pakkanen and Vaheri 1989; Pakkanen et al. 1987) and identical to ezrin (Gould et al. 1989).
Structure, Expression, and Conformational Regulation
Gene and Domain Organization
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