Integral plasma membrane proteins are stabilized by linkages to the cortical actin cytoskeleton, which structurally supports the membrane and contributes to processes such as endocytosis, exocytosis, and transmembrane signaling. The ERM (ezrin-radixin-moesin) family of proteins provides these structural linkages. The ERM proteins contain a 300-residue N-terminal domain, a 170-residue α-helical region, and a C-terminal 100-residue domain that contains F-actin binding sites. The N-terminal domain interacts with the cytoplasmic domain of CD44, the regulatory subunit of PKA, and the PDZ domain containing ERM-binding phosphoprotein (EBP-50). In polarized epithelial cells, EBP-50 links ezrin and the cytoplasmic regions of transmembrane proteins such as the cystic fibrosis transmembrane conductance regulator (CFTR) and the β2-adrenergic receptor. EBP50 contains two PDZ domains followed by a C-terminal tail. It colocalizes with ezrin in apical microvilli and is also thought to interact with the Na+-H+ exchanger NHE3 to confer cAMP-mediated inhibition of Na+-H+ exchange. Thus, EBP-50 mediates membrane attachment to the cytoskeleton and may also function in the regulation of ion exchange.
This antibody is routinely tested in western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.