Fas-associated Death Domain Protein and Caspase-8 Are Not Recruited to the Tumor Necrosis Factor Receptor 1 Signaling Complex during Tumor Necrosis Factor-induced Apoptosis *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 278, Issue: 28, Page: 25534-25541
2003
- 185Citations
- 102Captures
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Metrics Details
- Citations185
- Citation Indexes185
- 185
- CrossRef154
- Captures102
- Readers102
- 102
Article Description
Death receptors are a subfamily of the tumor necrosis factor (TNF) receptor subfamily. They are characterized by a death domain (DD) motif within their intracellular domain, which is required for the induction of apoptosis. Fas-associated death domain protein (FADD) is reported to be the universal adaptor used by death receptors to recruit and activate the initiator caspase-8. CD95, TNF-related apoptosis-inducing ligand (TRAIL-R1), and TRAIL-R2 bind FADD directly, whereas recruitment to TNF-R1 is indirect through another adaptor TNF receptor-associated death domain protein (TRADD). TRADD also binds two other adaptors receptor-interacting protein (RIP) and TNF-receptor-associated factor 2 (TRAF2), which are required for TNF-induced NF-κB and c-Jun N-terminal kinase activation, respectively. Analysis of the native TNF signaling complex revealed the recruitment of RIP, TRADD, and TRAF2 but not FADD or caspase-8. TNF failed to induce apoptosis in FADD- and caspase-8-deficient Jurkat cells, indicating that these apoptotic mediators were required for TNF-induced apoptosis. In an in vitro binding assay, the intracellular domain of TNF-R1 bound TRADD, RIP, and TRAF2 but did not bind FADD or caspase-8. Under the same conditions, the intracellular domain of both CD95 and TRAIL-R2 bound both FADD and caspase-8. Taken together these results suggest that apoptosis signaling by TNF is distinct from that induced by CD95 and TRAIL. Although caspase-8 and FADD are obligatory for TNF-mediated apoptosis, they are not recruited to a TNF-induced membrane-bound receptor signaling complex as occurs during CD95 or TRAIL signaling, but instead must be activated elsewhere within the cell.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819750674; http://dx.doi.org/10.1074/jbc.m303399200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037815277&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12721308; https://linkinghub.elsevier.com/retrieve/pii/S0021925819750674; http://www.jbc.org/lookup/doi/10.1074/jbc.M303399200; https://syndication.highwire.org/content/doi/10.1074/jbc.M303399200; https://dx.doi.org/10.1074/jbc.m303399200
Elsevier BV
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