Fas receptor (CD95, TNFRSF6) and Fas ligand (CD95L, Apo-1L, tumor necrosis factor ligand superfamily member 6) (Fas (for the receptor), FasL (for the ligand))

The Fas receptor (CD95, TNFRSF6) is a cell-surface death receptor in the tumor necrosis factor receptor superfamily, containing a death domain essential for mediating apoptosis through recruitment of FADD and activation of caspases when engaged by its natural ligand, Fas ligand (FasL/ CD95L). Fas ligand is a type-II transmembrane protein in the tumor necrosis factor ligand superfamily. Its binding to Fas receptor catalyzes formation of the death-inducing signaling complex (DISC), leading to caspase-8 and downstream effector caspase-3 activation, cell death, and immune privilege. Fas/FasL interactions tightly regulate T-cell lifespan, immune homeostasis, and the elimination of autoreactive lymphocytes. Dysregulation is linked to autoimmune lymphoproliferative syndromes, cancer escape, and transplantation rejection. Both molecules exist in membrane-bound and soluble forms, each with distinct biological activities and regulatory roles.

Other names

CD95APO-1TNFRSF6FasLCD95LApo-1LFASLG

Induction or inhibition of apoptosis by modulating receptor-ligand interaction (e.g. agonists trigger apoptosis; inhibitors block immune cell death). Modulation of immune cell activation and survival.