PEA-15-AA

PEA-15-AA is a double-mutated, unphosphorylatable form of the 15-kDa phosphoprotein PEA-15 (Phosphoprotein Enriched in Astrocytes-15). In this variant, the two major phosphorylation sites, Serine 104 and Serine 116, are substituted with alanine to prevent phosphorylation. PEA-15-AA acts as a potent antitumor agent by sequestering phosphorylated extracellular signal-regulated kinase (p-ERK) in the cytoplasm, thereby preventing its nuclear translocation and subsequent proliferative signaling. Additionally, it has been shown to inhibit the expression and nuclear localization of beta-catenin. Developed by researchers at the UT MD Anderson Cancer Center, PEA-15-AA has demonstrated significant inhibition of tumorigenesis, cell migration, and colony formation in ovarian cancer models both in vitro and in vivo, suggesting its potential as a therapeutic molecule for epithelial ovarian cancer.

Other names

double-unphosphorylated PEA-15Ser104Ala/Ser116Ala PEA-15 mutant