Abstract
ERM (ezrin/radixin/moesin) proteins, concentrated in actin rich cell-surface structures, cross-link actin filaments with the plasma membrane. Recent work using genetic approaches has revealed a surprising wealth of phenotypes and functions for ERMs in the context of both normal tissues and disease states. Such a wide array of phenotypes, from loss of epithelial integrity to disruption of embryonic anterior-posterior polarity, seems to suggest a wide range of molecular functions. They are involved in the formation of microvilli, cell-cell adhesion, maintenance of cell shape, cell motility, membrane trafficking and metastasis. The functions of ERM proteins are regulated by their conformational changes: the intramolecular interaction between the N- and C-terminal domains of ERM proteins masks several binding sites, leading to a dormant protein. Different activation signals regulate ERM proteins functions by modulating these intramolecular interactions.
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