TNFRSF1A | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | TNFRSF1A, CD120a, FPF, MS5, TBP1, TNF-R, TNF-R-I, TNF-R55, TNFAR, TNFR1, TNFR1-d2, TNFR55, TNFR60, p55, p55-R, p60, tumor necrosis factor receptor superfamily member 1A, TNF receptor superfamily member 1A | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 191190; MGI: 1314884; HomoloGene: 828; GeneCards: TNFRSF1A; OMA:TNFRSF1A - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Tumor necrosis factor receptor 1 (TNFR1), also known as tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) and CD120a, is a ubiquitous membrane receptor that binds tumor necrosis factor-alpha (TNFα).[5][6][7]
Function
[edit]The protein encoded by this gene is a member of the tumor necrosis factor receptor superfamily, which also contains TNFRSF1B. This protein is one of the major receptors for the tumor necrosis factor-alpha. This receptor can activate the transcription factor NF-κB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor.[8]
Clinical significance
[edit]Germline mutations of the extracellular domains of this receptor were found to be associated with the human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS) or periodic fever syndrome.[9] Impaired receptor clearance is thought to be a mechanism of the disease.
Mutations in the TNFRSF1A gene are associated with elevated risk of multiple sclerosis.[10]
Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder,[11] and high levels are associated with more severe psychotic symptoms.[12]
High serum levels are also associated with cognitive impairment and dementia.[13][14]
Interactions
[edit]TNFRSF1A has been shown to interact with:
See also
[edit]References
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- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030341 – Ensembl, May 2017
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- ^ a b Jiang Y, Woronicz JD, Liu W, Goeddel DV (1999). "Prevention of constitutive TNF receptor 1 signaling by silencer of death domains". Science. 283 (5401): 543–6. Bibcode:1999Sci...283..543J. doi:10.1126/science.283.5401.543. PMID 9915703.
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- ^ a b c Hsu H, Shu HB, Pan MG, Goeddel DV (1996). "TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways". Cell. 84 (2): 299–308. doi:10.1016/S0092-8674(00)80984-8. PMID 8565075. S2CID 13171355.
- ^ Zhang SQ, Kovalenko A, Cantarella G, Wallach D (2000). "Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation". Immunity. 12 (3): 301–11. doi:10.1016/S1074-7613(00)80183-1. PMID 10755617.
- ^ Chaudhary PM, Eby MT, Jasmin A, Kumar A, Liu L, Hood L (2000). "Activation of the NF-kappaB pathway by caspase 8 and its homologs". Oncogene. 19 (39): 4451–60. doi:10.1038/sj.onc.1203812. PMID 11002417.
- ^ a b Guo D, Dunbar JD, Yang CH, Pfeffer LM, Donner DB (1998). "Induction of Jak/STAT signaling by activation of the type 1 TNF receptor". J. Immunol. 160 (6): 2742–50. doi:10.4049/jimmunol.160.6.2742. PMID 9510175.
- ^ Miscia S, Marchisio M, Grilli A, Di Valerio V, Centurione L, Sabatino G, Garaci F, Zauli G, Bonvini E, Di Baldassarre A (2002). "Tumor necrosis factor alpha (TNF-alpha) activates Jak1/Stat3-Stat5B signaling through TNFR-1 in human B cells". Cell Growth Differ. 13 (1): 13–8. PMID 11801527.
- ^ Castellino AM, Parker GJ, Boronenkov IV, Anderson RA, Chao MV (1997). "A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase". J. Biol. Chem. 272 (9): 5861–70. doi:10.1074/jbc.272.9.5861. PMID 9038203.
- ^ Boldin MP, Mett IL, Wallach D (1995). "A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'". FEBS Lett. 367 (1): 39–44. doi:10.1016/0014-5793(95)00534-G. PMID 7601280. S2CID 21442471.
- ^ Dunbar JD, Song HY, Guo D, Wu LW, Donner DB (1997). "Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor: identity with subunit 2 of the 26S protease". J. Immunol. 158 (9): 4252–9. doi:10.4049/jimmunol.158.9.4252. PMID 9126987.
- ^ a b c Hsu H, Huang J, Shu HB, Baichwal V, Goeddel DV (1996). "TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex". Immunity. 4 (4): 387–96. doi:10.1016/S1074-7613(00)80252-6. PMID 8612133.
- ^ Kim JW, Choi EJ, Joe CO (2000). "Activation of death-inducing signaling complex (DISC) by pro-apoptotic C-terminal fragment of RIP". Oncogene. 19 (39): 4491–9. doi:10.1038/sj.onc.1203796. PMID 11002422.
- ^ Duan H, Dixit VM (1997). "RAIDD is a new 'death' adaptor molecule" (PDF). Nature. 385 (6611): 86–9. Bibcode:1997Natur.385...86D. doi:10.1038/385086a0. hdl:2027.42/62739. PMID 8985253. S2CID 4317538.
- ^ a b Blankenship JW, Varfolomeev E, Goncharov T, Fedorova AV, Kirkpatrick DS, Izrael-Tomasevic A, Phu L, Arnott D, Aghajan M, Zobel K, Bazan JF, Fairbrother WJ, Deshayes K, Vucic D (2009). "Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2(1)". Biochem. J. 417 (1): 149–60. doi:10.1042/BJ20081885. PMID 18939944.
- ^ Newton K, Matsumoto ML, Wertz IE, Kirkpatrick DS, Lill JR, Tan J, Dugger D, Gordon N, Sidhu SS, Fellouse FA, Komuves L, French DM, Ferrando RE, Lam C, Compaan D, Yu C, Bosanac I, Hymowitz SG, Kelley RF, Dixit VM (2008). "Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies". Cell. 134 (4): 668–78. doi:10.1016/j.cell.2008.07.039. PMID 18724939. S2CID 3955385.
- ^ Varfolomeev E, Goncharov T, Fedorova AV, Dynek JN, Zobel K, Deshayes K, Fairbrother WJ, Vucic D (2008). "c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation". J. Biol. Chem. 283 (36): 24295–9. doi:10.1074/jbc.C800128200. PMC 3259840. PMID 18621737.
- ^ Liou ML, Liou HC (1999). "The ubiquitin-homology protein, DAP-1, associates with tumor necrosis factor receptor (p60) death domain and induces apoptosis". J. Biol. Chem. 274 (15): 10145–53. doi:10.1074/jbc.274.15.10145. PMID 10187798.
- ^ Okura T, Gong L, Kamitani T, Wada T, Okura I, Wei CF, Chang HM, Yeh ET (1996). "Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin". J. Immunol. 157 (10): 4277–81. doi:10.4049/jimmunol.157.10.4277. PMID 8906799.
- ^ a b Shu HB, Takeuchi M, Goeddel DV (1996). "The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13973–8. Bibcode:1996PNAS...9313973S. doi:10.1073/pnas.93.24.13973. PMC 19479. PMID 8943045.
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- ^ Soond SM, Terry JL, Colbert JD, Riches DW (2003). "TRUSS, a novel tumor necrosis factor receptor 1 scaffolding protein that mediates activation of the transcription factor NF-kappaB". Mol. Cell. Biol. 23 (22): 8334–44. doi:10.1128/MCB.23.22.8334-8344.2003. PMC 262424. PMID 14585990.
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Further reading
[edit]- Rath PC, Aggarwal BB (2000). "TNF-induced signaling in apoptosis". J. Clin. Immunol. 19 (6): 350–64. doi:10.1023/A:1020546615229. PMID 10634209. S2CID 23194856.
- Chen G, Goeddel DV (2002). "TNF-R1 signaling: a beautiful pathway". Science. 296 (5573): 1634–5. Bibcode:2002Sci...296.1634C. doi:10.1126/science.1071924. PMID 12040173. S2CID 25321662.
- Kollias G, Kontoyiannis D (2003). "Role of TNF/TNFR in autoimmunity: specific TNF receptor blockade may be advantageous to anti-TNF treatments". Cytokine Growth Factor Rev. 13 (4–5): 315–21. doi:10.1016/S1359-6101(02)00019-9. PMID 12220546.
- Dodé C, Cuisset L, Delpech M, Grateau G (2003). "TNFRSF1A-associated periodic syndrome (TRAPS), Muckle–Wells syndrome (MWS) and renal amyloidosis". J. Nephrol. 16 (3): 435–7. PMID 12832748.
- Stojanov S, McDermott MF (2007). "The tumour necrosis factor receptor-associated periodic syndrome: current concepts". Expert Reviews in Molecular Medicine. 7 (22): 1–18. doi:10.1017/S1462399405009749. PMID 16216134. S2CID 35803989.
- Rezaei N (2007). "TNF-receptor-associated periodic syndrome (TRAPS): an autosomal dominant multisystem disorder". Clin. Rheumatol. 25 (6): 773–7. doi:10.1007/s10067-005-0198-6. PMID 16447098. S2CID 41808394.
External links
[edit]- TNFRSF1A+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Overview of all the structural information available in the PDB for UniProt: P19438 (Tumor necrosis factor receptor superfamily member 1A) at the PDBe-KB.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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