TAX1BP3 is a small, highly conserved protein that contains a single PDZ (PSD-95/Discs large/ZO-1 homologous) domain . Unlike most PDZ domain proteins, which often act as scaffolds and contain multiple PDZ domains, TIP-1 is essentially just the PDZ domain . This unique structure suggests that TIP-1 may function as an inhibitor by either separating PDZ binding motifs from their normal targets or preventing the protein from migrating away from the cytosol .
The PDZ domain promotes protein-protein interactions that are crucial for various cellular processes, including cell signaling, adhesion, protein scaffolding, and receptor and ion transporter functions . TAX1BP3 interacts with a large number of target proteins involved in signaling pathways, such as Rho A and glutaminase L . It also acts as a negative regulator of the Wnt/beta-catenin signaling pathway .
TAX1BP3 plays several important roles in cellular functions:
The human recombinant TAX1BP3 protein is produced in E. coli as a single, non-glycosylated polypeptide chain containing 144 amino acids and has a molecular mass of approximately 15.8 kDa . The recombinant protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques .
Given its involvement in critical cellular processes and disease mechanisms, TAX1BP3 is a significant protein for both clinical and research applications. Its role in cancer cell behavior makes it a potential target for therapeutic interventions. Additionally, its regulatory functions in signaling pathways highlight its importance in understanding cellular communication and disease progression.