Molecules involved in ERM (ezrin-radixin-moesin) based attachment of membrane proteins to the cortical cytoskeleton in cell surface structures have been identified. In lymphocytes, a direct interaction is seen with extracellular matrix receptors and intercellular adhesion molecules. In polarized epithelial cells, an adaptor molecule named EBP50 provides a bridge between the amino-terminal domain of ezrin and the cytoplasmic regions of plasma membrane proteins, including the cystic fibrosis transmembrane conductance regulator (CFTR) and the β₂ adrenergic receptor. ERM proteins are conformationally regulated — binding sites for EBP50 and F actin are masked in the dormant molecules and activation leads to exposure of these sites. The mechanism of activation, however, remains to be fully elucidated. ERM proteins also play a role in the Rho and Rac signaling pathways: activated ERM proteins can dissociate Rho-GDI (GDP dissociation inhibitor) from Rho and thereby activate Rho-dependent pathways.