Biology:Tumor necrosis factor receptor 1
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Short description: Membrane receptor protein found in humans
 Generic protein structure example |
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).[1][2][3]
Function
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.[4]
Clinical significance
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.[5] 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.[6]
Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder,[7] and high levels are associated with more severe psychotic symptoms.[8]
High serum levels are also associated with cognitive impairment and dementia.[9][10]
Interactions
TNFRSF1A has been shown to interact with:
- BAG4,[11][12]
- CASP10,[13][14]
- FADD,[13][15]
- IKK2,[16][17]
- JAK1,[18][19]
- JAK2,[18]
- PIP4K2B,[20]
- PSMD2,[21][22]
- RIPK1,[23][24][25][26][27][28]
- SUMO1,[29][30]
- TRADD[11][15][23][26][31][32][33]
- TRAF2,[15][23][31]
- TRPC4AP,[34]
- TNF,[35][36] and
- UBE2I.[37]
See also
References
- ↑ "Chromosomal location of the human tumor necrosis factor receptor genes". Cytogenet Cell Genet 57 (2–3): 117–8. November 1991. doi:10.1159/000133127. PMID 1655358.
- ↑ "Molecular cloning and expression of a receptor for human tumor necrosis factor". Cell 61 (2): 361–70. June 1990. doi:10.1016/0092-8674(90)90816-W. PMID 2158863. http://www.escholarship.org/uc/item/39j2j0h2.
- ↑ Offermanns, Stefan; Rosenthal, Walter (2008). Encyclopedia of Molecular Pharmacology, Vol. 1 (2nd ed.). Heidelberg, Germany: Springer. p. 1248. ISBN 9783540389163. https://books.google.com/books?id=iwwo5gx8aX8C.
- ↑ "Entrez Gene: TNFRSF1A tumor necrosis factor receptor superfamily, member 1A". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7132.
- ↑ "Multiple sclerosis. TNFRSF1A, TRAPS and multiple sclerosis". Nat Rev Neurol 5 (10): 528–9. October 2009. doi:10.1038/nrneurol.2009.154. PMID 19794511.
- ↑ International Multiple Sclerosis Genetics Consortium (2011). "The genetic association of variants in CD6, TNFRSF1A and IRF8 to multiple sclerosis: a multicenter case-control study". PLOS ONE 6 (4): e18813. doi:10.1371/journal.pone.0018813. PMID 21552549. Bibcode: 2011PLoSO...618813..
- ↑ "Similar immune profile in bipolar disorder and schizophrenia: selective increase in soluble tumor necrosis factor receptor I and von Willebrand factor". Bipolar Disord 11 (7): 726–34. November 2009. doi:10.1111/j.1399-5618.2009.00757.x. PMID 19839997.
- ↑ "Interleukin 1 receptor antagonist and soluble tumor necrosis factor receptor 1 are associated with general severity and psychotic symptoms in schizophrenia and bipolar disorder". Schizophr. Res. 145 (1–3): 36–42. April 2013. doi:10.1016/j.schres.2012.12.023. PMID 23403415.
- ↑ "Soluble TNF receptors are associated with Aβ metabolism and conversion to dementia in subjects with mild cognitive impairment". Neurobiol. Aging 31 (11): 1877–84. November 2010. doi:10.1016/j.neurobiolaging.2008.10.012. PMID 19070941.
- ↑ "Higher serum sTNFR1 level predicts conversion from mild cognitive impairment to Alzheimer's disease". J. Alzheimers Dis. 22 (4): 1305–11. 2010. doi:10.3233/JAD-2010-100921. PMID 20930310.
- ↑ 11.0 11.1 "Prevention of constitutive TNF receptor 1 signaling by silencer of death domains". Science 283 (5401): 543–6. 1999. doi:10.1126/science.283.5401.543. PMID 9915703. Bibcode: 1999Sci...283..543J.
- ↑ "Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain". Mol. Cell. Biol. 22 (8): 2536–43. 2002. doi:10.1128/MCB.22.8.2536-2543.2002. PMID 11909948.
- ↑ 13.0 13.1 "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. 2005. doi:10.1074/jbc.M411781200. PMID 15659383.
- ↑ "Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling". J. Biol. Chem. 272 (10): 6578–83. 1997. doi:10.1074/jbc.272.10.6578. PMID 9045686.
- ↑ 15.0 15.1 15.2 "TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways". Cell 84 (2): 299–308. 1996. doi:10.1016/S0092-8674(00)80984-8. PMID 8565075.
- ↑ "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. 2000. doi:10.1016/S1074-7613(00)80183-1. PMID 10755617.
- ↑ "Activation of the NF-kappaB pathway by caspase 8 and its homologs". Oncogene 19 (39): 4451–60. 2000. doi:10.1038/sj.onc.1203812. PMID 11002417.
- ↑ 18.0 18.1 "Induction of Jak/STAT signaling by activation of the type 1 TNF receptor". J. Immunol. 160 (6): 2742–50. 1998. doi:10.4049/jimmunol.160.6.2742. PMID 9510175.
- ↑ "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. 2002. PMID 11801527.
- ↑ "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. 1997. doi:10.1074/jbc.272.9.5861. PMID 9038203.
- ↑ "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. 1995. doi:10.1016/0014-5793(95)00534-G. PMID 7601280.
- ↑ "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. 1997. doi:10.4049/jimmunol.158.9.4252. PMID 9126987.
- ↑ 23.0 23.1 23.2 "TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex". Immunity 4 (4): 387–96. 1996. doi:10.1016/S1074-7613(00)80252-6. PMID 8612133.
- ↑ "Activation of death-inducing signaling complex (DISC) by pro-apoptotic C-terminal fragment of RIP". Oncogene 19 (39): 4491–9. 2000. doi:10.1038/sj.onc.1203796. PMID 11002422.
- ↑ "RAIDD is a new 'death' adaptor molecule". Nature 385 (6611): 86–9. 1997. doi:10.1038/385086a0. PMID 8985253. Bibcode: 1997Natur.385...86D. https://deepblue.lib.umich.edu/bitstream/2027.42/62739/1/385086a0.pdf.
- ↑ 26.0 26.1 "Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2(1)". Biochem. J. 417 (1): 149–60. 2009. doi:10.1042/BJ20081885. PMID 18939944.
- ↑ "Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies". Cell 134 (4): 668–78. 2008. doi:10.1016/j.cell.2008.07.039. PMID 18724939.
- ↑ "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. 2008. doi:10.1074/jbc.C800128200. PMID 18621737.
- ↑ "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. 1999. doi:10.1074/jbc.274.15.10145. PMID 10187798.
- ↑ "Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin". J. Immunol. 157 (10): 4277–81. 1996. doi:10.4049/jimmunol.157.10.4277. PMID 8906799.
- ↑ 31.0 31.1 "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. 1996. doi:10.1073/pnas.93.24.13973. PMID 8943045. Bibcode: 1996PNAS...9313973S.
- ↑ "Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling". J. Biol. Chem. 274 (15): 10203–12. 1999. doi:10.1074/jbc.274.15.10203. PMID 10187805.
- ↑ "The receptor for the cytotoxic ligand TRAIL". Science 276 (5309): 111–3. 1997. doi:10.1126/science.276.5309.111. PMID 9082980.
- ↑ "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. 2003. doi:10.1128/MCB.23.22.8334-8344.2003. PMID 14585990.
- ↑ "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. 2004. doi:10.1038/ncb1086. PMID 14743216.
- ↑ "The TNF receptor 1: a split personality complex". Cell 114 (2): 148–50. 2003. doi:10.1016/s0092-8674(03)00561-0. PMID 12887914.
- ↑ "hUBC9 associates with MEKK1 and type I TNF-alpha receptor and stimulates NFkappaB activity". FEBS Lett. 425 (3): 431–5. 1998. doi:10.1016/S0014-5793(98)00287-7. PMID 9563508.
Further reading
- "TNF-induced signaling in apoptosis". J. Clin. Immunol. 19 (6): 350–64. 2000. doi:10.1023/A:1020546615229. PMID 10634209.
- "TNF-R1 signaling: a beautiful pathway". Science 296 (5573): 1634–5. 2002. doi:10.1126/science.1071924. PMID 12040173. Bibcode: 2002Sci...296.1634C.
- "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. 2003. doi:10.1016/S1359-6101(02)00019-9. PMID 12220546.
- "TNFRSF1A-associated periodic syndrome (TRAPS), Muckle–Wells syndrome (MWS) and renal amyloidosis". J. Nephrol. 16 (3): 435–7. 2003. PMID 12832748.
- "The tumour necrosis factor receptor-associated periodic syndrome: current concepts". Expert Reviews in Molecular Medicine 7 (22): 1–18. 2007. doi:10.1017/S1462399405009749. PMID 16216134.
- 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.
External links
- TNFRSF1A+protein,+human at the US 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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