FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2.

By M. Sprick, Markus A. Weigand, E. Rieser, C. Rauch, P. Juo, J. Blenis, P. Krammer, H. Walczak. Immunity, 2000

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A decade of caspases (2003, background): “For example, caspase-8-deficient Jurkat cells are completely resistant to Fas and TRAIL-R2 and partially resistant to TNFainduced apoptosis (Juo et al., 1998; Bodmer et al., 2000; Sprick et al., 2000).”
The E-Cadherin and N-Cadherin Switch in Epithelial-to-Mesenchymal Transition: Signaling, Therapeutic Implications, and Challenges (2019, background): “Ligated death receptor (DR) 4 and DR5 attach to Fas-associated death domain (FADD) then caspase-8 to become a death-inducing signaling complex (DISC) [70,71].”
CD95's deadly mission in the immune system (2000, background): “Signalling by other death receptors Signalling of apoptosis by other members of the death receptor subfamily seems to follow the same basic rules and is initiated by the same sequential step”
Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling. (2009, neutral): “As previously established, ligand binding induces receptor clustering and recruitment of FADD and caspase-8, forming an apical DISC (Kischkel et al., 2000; Sprick et al., 2000).”