Glucocorticoid Modulatory Element Binding Protein 2 (GMEB2)

GMEB2 contains an N-terminal KDWK domain, and a highly acidic C terminus that likely forms a coiled-coil structure. Recombinant and endogenous GMEB2 share identical mobilities when analyzed by SDS/PAGE, indicating a lack of posttranslational modification. Within the N-terminal KDWK domain, GMEB2 shares about 80% identity with GMEB1; overall, they share about 40% identity.The authors found that GMEB2 and GMEB1 self-associate when expressed alone, and that they form heterodimers when expressed together. Cross-linking experiments indicated that no higher-order multimers were formed. Each protein was active in promoter activation assays, and the complex bound regulatory elements within the promoter regions of tyrosine animotransferase and the transferrin receptor gene.