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The **death receptor pathway** refers to a group of cell surface receptors—primarily **Fas** (CD95), **TRAIL receptors** (**DR4/TRAIL-R1**, **DR5/TRAIL-R2**), and the **tumor necrosis factor alpha receptor 1** (**TNFR1**)—that are activated by their respective ligands (**Fas ligand [FasL]**, **TRAIL**, and **TNF-alpha**) released from immune effector cells such as natural killer cells. These receptors belong to the tumor necrosis factor (TNF) superfamily and share a conserved intracellular "death domain" that initiates apoptotic signaling upon ligand engagement. Activation leads to recruitment of adaptor proteins like FADD and subsequent activation of caspases, resulting in programmed cell death. This mechanism is crucial for immune surveillance against tumors and infected cells but can also contribute to pathological tissue damage if dysregulated[2][3][4].
Induction of apoptosis via activation of caspase cascade through death domain signaling upon ligand binding[2][3][4]
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