Fas receptor (FAS)

The Fas receptor (CD95) is a transmembrane protein and a member of the tumor necrosis factor receptor (TNFR) superfamily that plays a central role in the regulation of programmed cell death (UniProt: P25446). Upon binding to its ligand (FasL), the receptor trimerizes and recruits the adapter protein FADD and procaspase-8 to form the death-inducing signaling complex (DISC), which initiates the extrinsic apoptotic pathway (PubMed: 17534408). In multiple myeloma, the Fas pathway is frequently impaired, allowing malignant plasma cells to evade immune surveillance and chemotherapy-induced apoptosis (PubMed: 25852056). While direct systemic activation of Fas is precluded by severe hepatotoxicity, many current myeloma therapies, such as proteasome inhibitors (e.g., bortezomib), exert their effects in part by restoring Fas sensitivity or upregulating Fas expression on the cell surface (PubMed: 15153485). Consequently, the Fas pathway remains a significant focal point for understanding drug resistance and developing combination strategies in hematologic malignancies.

Other names

CD95APO-1Tumor necrosis factor receptor superfamily member 6TNFRSF6APT1FASLG receptor

Activation of the extrinsic apoptotic pathway through the formation of the death-inducing signaling complex (DISC), leading to the activation of caspase-8 and subsequent executioner caspases.