Biology:Death receptor 4
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Short description: Protein found in humans
 Generic protein structure example |
Death receptor 4 (DR4), also known as TRAIL receptor 1 (TRAILR1) and tumor necrosis factor receptor superfamily member 10A (TNFRSF10A), is a cell surface receptor of the TNF-receptor superfamily that binds TRAIL and mediates apoptosis.[1][2]
Function
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL), and thus transduces cell death signal and induces cell apoptosis.[3]
Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein.[4]
Interactions
TNFRSF10A has been shown to interact with DAP3.[5]
References
- ↑ "TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL". EMBO J 16 (17): 5386–97. Dec 1997. doi:10.1093/emboj/16.17.5386. PMID 9311998.
- ↑ "The receptor for the cytotoxic ligand TRAIL". Science 276 (5309): 111–3. April 1997. doi:10.1126/science.276.5309.111. PMID 9082980.
- ↑ "Entrez Gene: TNFRSF10A tumor necrosis factor receptor superfamily, member 10a". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8797.
- ↑ "FADD is required for DR4- and DR5-mediated apoptosis: lack of trail-induced apoptosis in FADD-deficient mouse embryonic fibroblasts.". J. Biol. Chem. 275 (33): 25065–8. 2000. doi:10.1074/jbc.C000284200. PMID 10862756.
- ↑ Miyazaki, T; Reed J C (June 2001). "A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins". Nat. Immunol. 2 (6): 493–500. doi:10.1038/88684. ISSN 1529-2908. PMID 11376335.
Further reading
- "Following a TRAIL: update on a ligand and its five receptors.". Cell Res. 14 (5): 359–72. 2005. doi:10.1038/sj.cr.7290236. PMID 15538968.
- "HLA-DR polymorphism affects the interaction with CD4.". J. Exp. Med. 182 (3): 733–41. 1995. doi:10.1084/jem.182.3.733. PMID 7650480.
- "Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL.". J. Biol. Chem. 272 (41): 25417–20. 1997. doi:10.1074/jbc.272.41.25417. PMID 9325248.
- "Characterization of two receptors for TRAIL.". FEBS Lett. 416 (3): 329–34. 1997. doi:10.1016/S0014-5793(97)01231-3. PMID 9373179. https://serval.unil.ch/resource/serval:BIB_25D695CC2FFE.P001/REF.pdf.
- "A novel receptor for Apo2L/TRAIL contains a truncated death domain.". Curr. Biol. 7 (12): 1003–6. 1998. doi:10.1016/S0960-9822(06)00422-2. PMID 9382840.
- "Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappaB pathway.". Immunity 7 (6): 821–30. 1998. doi:10.1016/S1074-7613(00)80400-8. PMID 9430227.
- "TRAIL receptors 1 (DR4) and 2 (DR5) signal FADD-dependent apoptosis and activate NF-kappaB.". Immunity 7 (6): 831–6. 1998. doi:10.1016/S1074-7613(00)80401-X. PMID 9430228. https://serval.unil.ch/notice/serval:BIB_1D571B98E298.
- "Human collagen II peptide 256-271 preferentially binds to HLA-DR molecules associated with susceptibility to rheumatoid arthritis.". Immunogenetics 49 (1): 36–44. 1999. doi:10.1007/s002510050461. PMID 9811967.
- "c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and activates nuclear factor-kappaB.". J. Biol. Chem. 274 (29): 20127–32. 1999. doi:10.1074/jbc.274.29.20127. PMID 10400625.
- "Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5.". Mol. Cell 4 (4): 563–71. 1999. doi:10.1016/S1097-2765(00)80207-5. PMID 10549288.
- "Increased expression of death receptors 4 and 5 synergizes the apoptosis response to combined treatment with etoposide and TRAIL.". Mol. Cell. Biol. 20 (1): 205–12. 2000. doi:10.1128/MCB.20.1.205-212.2000. PMID 10594023.
- "A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins.". Nat. Immunol. 2 (6): 493–500. 2001. doi:10.1038/88684. PMID 11376335.
- "CD95 and TRAIL receptor-mediated activation of protein kinase C and NF-kappaB contributes to apoptosis resistance in ductal pancreatic adenocarcinoma cells.". Oncogene 20 (31): 4258–69. 2001. doi:10.1038/sj.onc.1204559. PMID 11464292.
- "Lack of tumor necrosis factor-related apoptosis-inducing ligand but presence of its receptors in the human brain.". J. Neurosci. 22 (4): RC209. 2002. doi:10.1523/JNEUROSCI.22-04-j0001.2002. PMID 11844843.
- "Expression of TNF-related apoptosis-inducing ligand (TRAIL) and its receptors in gastric carcinoma and tumor-infiltrating lymphocytes: a possible mechanism of immune evasion of the tumor.". J. Cancer Res. Clin. Oncol. 128 (2): 73–9. 2002. doi:10.1007/s004320100292. PMID 11862476.
- "Evidence that the human death receptor 4 is regulated by activator protein 1.". Oncogene 21 (20): 3121–9. 2002. doi:10.1038/sj.onc.1205430. PMID 12082627.
- "Mitogen-activated protein kinase/extracellular signal-regulated kinase signaling in activated T cells abrogates TRAIL-induced apoptosis upstream of the mitochondrial amplification loop and caspase-8.". J. Immunol. 169 (6): 2851–60. 2002. doi:10.4049/jimmunol.169.6.2851. PMID 12218097.
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