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.
原厂资料:
注意事项:
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.