TRAIL R2/TNFRSF10B Protein, Human

The TRAIL R2/TNFRSF10B Protein functions as a receptor for the cytotoxic ligand TNFSF10/TRAIL. Upon ligand binding, the adapter molecule FADD recruits caspase-8 to the activated receptor, forming the death-inducing signaling complex (DISC), which triggers caspase-8 proteolytic activation and initiates the subsequent cascade of caspases, mediating apoptosis. Additionally, TRAIL R2/TNFRSF10B promotes the activation of NF-kappa-B and is essential for endoplasmic reticulum (ER) stress-induced apoptosis. In its monomeric state, it can interact with TRADD and RIPK1, and in the absence of stimulation, it interacts with BIRC2, DDX3X, and GSK3B. Stimulation of the receptor enhances interactions with BIRC2 and DDX3X, accompanied by their cleavage. Notably, TRAIL R2/TNFRSF10B can also interact with the HCMV protein UL141, preventing cell surface expression, where two TNFRSF10B monomers interact with a UL141 homodimer, and three TNFRSF10B molecules interact with TNFSF10 homotrimer. These intricate interactions underline the multifaceted role of TRAIL R2/TNFRSF10B in apoptotic and signaling pathways.