RWDD4 is implicated in bladder cancer (BCa) progression through its regulation by miR-506, a tumor-suppressive microRNA. Studies demonstrate:
miR-506 Expression: Downregulated in BCa tissues and cell lines (T24, J82, UM-UC-3) compared to normal bladder epithelial cells (SV-HUC-1) .
Functional Impact: Overexpression of miR-506 inhibits BCa cell proliferation, migration, invasion, and epithelial-to-mesenchymal transition (EMT) .
Luciferase Assay: miR-506 directly binds the 3′UTR of RWDD4, suppressing its expression .
EMT Regulation: miR-506 upregulates E-cadherin and reduces N-cadherin/Vimentin, halting mesenchymal transition .
RWDD4 belongs to the RWD domain-containing protein family, characterized by conserved motifs implicated in protein interactions. Sequence alignments reveal structural homology across species:
The RWD domain facilitates interactions with signaling complexes, though specific targets remain unclear .
While comprehensive tissue expression data for RWDD4 is limited, studies suggest its involvement in bladder tissue. The Human Protein Atlas reports its presence in bladder cell lines, with ongoing single-cell and cancer-specific analyses . Further studies are needed to map its tissue-specific roles.
RWDD4’s dysregulation in BCa positions it as a potential therapeutic target. Strategies include:
miR-506 Mimics: Restoring miR-506 expression to suppress RWDD4 and inhibit EMT.
siRNA Knockdown: Directly targeting RWDD4 to mimic miR-506’s anti-tumor effects.
The exact function of RWDD4 is not fully understood, but proteins containing the RWD domain are generally involved in protein-protein interactions and may play roles in signal transduction, cell cycle regulation, and other critical cellular processes. The RWD domain itself is named after three proteins where it was first identified: RING finger-containing proteins, WD-repeat-containing proteins, and DEAD-like helicases.
Recombinant RWDD4 is used in various research applications, including:
Recombinant RWDD4 is produced using bacterial expression systems, such as E. coli. The protein is then purified using affinity chromatography techniques, which exploit the fusion tag added to the protein. The final product is typically supplied in a buffer solution containing Tris-HCl, NaCl, glycerol, and DTT to maintain stability and activity .