Basic leucine zipper and W2 domain-containing protein 2 (BZW2)

Basic leucine zipper and W2 domain-containing protein 2 (BZW2) is a cytoplasmic protein encoded by the BZW2 gene, highly conserved from bacteria to mammals. Its primary structure features a leucine zipper motif followed by an eIF5C domain, making it a member of the basic-region leucine zipper superfamily and an eIF5 mimetic. BZW2 regulates translation initiation by competing with eIF5 for eIF2 interaction; this influences start codon selection and ensures preference for canonical translation start sites (AUG). In oncogenesis, BZW2 is upregulated in multiple malignancies and promotes tumor growth, migration, invasion, and resistance to apoptosis via activation of oncogenic signaling pathways (c-Myc, AKT/mTOR, Wnt/β-catenin). BZW2 also interacts with viral proteins such as SARS-CoV-2 nsp8, suggesting roles in host-pathogen interaction. Its broad physiological function and implication in disease make BZW2 a promising, though challenging, candidate for therapeutic intervention and biomarker development[1][2][3][4][5].

Other names

eIF5-mimic protein 15MP1HSPC028MST017MSTP017Basic leucine zipper and W2 domains 2Eukaryotic translation factor 5

Translation inhibition via competition with eIF5 for eIF2 binding; Regulation of canonical versus non-canonical start site translation; Oncogenic cascade modulation by promoting degradation of GSK3β, activating Wnt/β-catenin; Upregulation of c-Myc and multiple growth-promoting pathways.