FADD
![](/Images/godic/202501/12/FADD_based_on_pdb_file_2GF52522.gif")
![](/Images/godic/202501/12/PBB_GE_FADD_202535_at_tn2522.png")
![Extrinsic apoptosis pathway: The Fas receptor (FasR) is stimulated by Fas ligand (FasL), recruiting FADD to the FasR via an interaction between the death domains (DD) of both molecules. Procaspase 8 is recruited to FADD and interacts via the death effector domains (DED) of both molecules. This results in the cleavage and activation of procaspase 8, forming caspase 8, which goes on to cleave and activate other caspases such as procaspase 3 to initiate the caspase cascade which leads to cell death.](/Images/godic/202501/12/Extrinsic_apoptosis2522.jpg")
![Regulation of FADD by MKRN1: MKRN1 ubiquitinylates FADD targeting it for degradation by the 26S proteosome. As it is degraded, FADD can no longer bind to the Fas receptor (Fas R) to induce apoptosis.](/Images/godic/202501/12/Regulation_of_FADD_by_MKRN12522.png")
Fas-Associated protein with Death Domain (FADD), also called MORT1, is encoded by the FADD gene on the 11q13.3 region of chromosome 11 in humans.
FADD is an adaptor protein that bridges members of the tumor necrosis factor receptor superfamily, such as the Fas-receptor, to procaspases 8 and 10 to form the death-inducing signaling complex (DISC) during apoptosis. As well as its most well known role in apoptosis, FADD has also been seen to play a role in other processes including proliferation, cell cycle regulation and development.