Biology:Tumor necrosis factor receptor 1

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Short description: Membrane receptor protein found in humans

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
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:

See also

References

  1. ↑ "Chromosomal location of the human tumor necrosis factor receptor genes". Cytogenetics and Cell Genetics 57 (2–3): 117–118. November 1991. doi:10.1159/000133127. PMID 1655358. 
  2. ↑ "Molecular cloning and expression of a receptor for human tumor necrosis factor". Cell 61 (2): 361–370. April 1990. doi:10.1016/0092-8674(90)90816-W. PMID 2158863. https://www.escholarship.org/uc/item/39j2j0h2. 
  3. ↑ Encyclopedia of Molecular Pharmacology. 1 (2nd ed.). Heidelberg, Germany: Springer. 2008. p. 1248. ISBN 978-3-540-38916-3. https://books.google.com/books?id=iwwo5gx8aX8C. 
  4. ↑ "Entrez Gene: TNFRSF1A tumor necrosis factor receptor superfamily, member 1A". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=7132. 
  5. ↑ "Multiple sclerosis. TNFRSF1A, TRAPS and multiple sclerosis". Nature Reviews. Neurology 5 (10): 528–529. October 2009. doi:10.1038/nrneurol.2009.154. PMID 19794511. 
  6. ↑ International Multiple Sclerosis Genetics Consortium (April 2011). "The genetic association of variants in CD6, TNFRSF1A and IRF8 to multiple sclerosis: a multicenter case-control study". PLOS ONE 6 (4). doi:10.1371/journal.pone.0018813. PMID 21552549. Bibcode: 2011PLoSO...618813.. 
  7. ↑ "Similar immune profile in bipolar disorder and schizophrenia: selective increase in soluble tumor necrosis factor receptor I and von Willebrand factor". Bipolar Disorders 11 (7): 726–734. November 2009. doi:10.1111/j.1399-5618.2009.00757.x. PMID 19839997. 
  8. ↑ "Interleukin 1 receptor antagonist and soluble tumor necrosis factor receptor 1 are associated with general severity and psychotic symptoms in schizophrenia and bipolar disorder". Schizophrenia Research 145 (1–3): 36–42. April 2013. doi:10.1016/j.schres.2012.12.023. PMID 23403415. 
  9. ↑ "Soluble TNF receptors are associated with Aβ metabolism and conversion to dementia in subjects with mild cognitive impairment". Neurobiology of Aging 31 (11): 1877–1884. November 2010. doi:10.1016/j.neurobiolaging.2008.10.012. PMID 19070941. 
  10. ↑ "Higher serum sTNFR1 level predicts conversion from mild cognitive impairment to Alzheimer's disease". Journal of Alzheimer's Disease 22 (4): 1305–1311. 2010. doi:10.3233/JAD-2010-100921. PMID 20930310. 
  11. ↑ 11.0 11.1 "Prevention of constitutive TNF receptor 1 signaling by silencer of death domains". Science 283 (5401): 543–546. January 1999. doi:10.1126/science.283.5401.543. PMID 9915703. Bibcode: 1999Sci...283..543J. 
  12. ↑ "Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain". Molecular and Cellular Biology 22 (8): 2536–2543. April 2002. doi:10.1128/MCB.22.8.2536-2543.2002. PMID 11909948. 
  13. ↑ 13.0 13.1 "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". The Journal of Biological Chemistry 280 (12): 11641–11647. March 2005. doi:10.1074/jbc.M411781200. PMID 15659383. 
  14. ↑ "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". The Journal of Biological Chemistry 272 (10): 6578–6583. March 1997. doi:10.1074/jbc.272.10.6578. PMID 9045686. 
  15. ↑ 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. January 1996. doi:10.1016/S0092-8674(00)80984-8. PMID 8565075. 
  16. ↑ "Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation". Immunity 12 (3): 301–311. March 2000. doi:10.1016/S1074-7613(00)80183-1. PMID 10755617. 
  17. ↑ "Activation of the NF-kappaB pathway by caspase 8 and its homologs". Oncogene 19 (39): 4451–4460. September 2000. doi:10.1038/sj.onc.1203812. PMID 11002417. 
  18. ↑ 18.0 18.1 "Induction of Jak/STAT signaling by activation of the type 1 TNF receptor". Journal of Immunology 160 (6): 2742–2750. March 1998. doi:10.4049/jimmunol.160.6.2742. PMID 9510175. 
  19. ↑ "Tumor necrosis factor alpha (TNF-alpha) activates Jak1/Stat3-Stat5B signaling through TNFR-1 in human B cells". Cell Growth & Differentiation 13 (1): 13–18. January 2002. PMID 11801527. 
  20. ↑ "A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase". The Journal of Biological Chemistry 272 (9): 5861–5870. February 1997. doi:10.1074/jbc.272.9.5861. PMID 9038203. 
  21. ↑ "A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'". FEBS Letters 367 (1): 39–44. June 1995. doi:10.1016/0014-5793(95)00534-G. PMID 7601280. Bibcode: 1995FEBSL.367...39B. 
  22. ↑ "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". Journal of Immunology 158 (9): 4252–4259. May 1997. doi:10.4049/jimmunol.158.9.4252. PMID 9126987. 
  23. ↑ 23.0 23.1 23.2 "TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex". Immunity 4 (4): 387–396. April 1996. doi:10.1016/S1074-7613(00)80252-6. PMID 8612133. 
  24. ↑ "Activation of death-inducing signaling complex (DISC) by pro-apoptotic C-terminal fragment of RIP". Oncogene 19 (39): 4491–4499. September 2000. doi:10.1038/sj.onc.1203796. PMID 11002422. 
  25. ↑ "RAIDD is a new 'death' adaptor molecule". Nature 385 (6611): 86–89. January 1997. doi:10.1038/385086a0. PMID 8985253. Bibcode: 1997Natur.385...86D. 
  26. ↑ 26.0 26.1 "Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2(1)". The Biochemical Journal 417 (1): 149–160. January 2009. doi:10.1042/BJ20081885. PMID 18939944. 
  27. ↑ "Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies". Cell 134 (4): 668–678. August 2008. doi:10.1016/j.cell.2008.07.039. PMID 18724939. 
  28. ↑ "c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation". The Journal of Biological Chemistry 283 (36): 24295–24299. September 2008. doi:10.1074/jbc.C800128200. PMID 18621737. 
  29. ↑ "The ubiquitin-homology protein, DAP-1, associates with tumor necrosis factor receptor (p60) death domain and induces apoptosis". The Journal of Biological Chemistry 274 (15): 10145–10153. April 1999. doi:10.1074/jbc.274.15.10145. PMID 10187798. 
  30. ↑ "Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin". Journal of Immunology 157 (10): 4277–4281. November 1996. doi:10.4049/jimmunol.157.10.4277. PMID 8906799. 
  31. ↑ 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". Proceedings of the National Academy of Sciences of the United States of America 93 (24): 13973–13978. November 1996. doi:10.1073/pnas.93.24.13973. PMID 8943045. Bibcode: 1996PNAS...9313973S. 
  32. ↑ "Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling". The Journal of Biological Chemistry 274 (15): 10203–10212. April 1999. doi:10.1074/jbc.274.15.10203. PMID 10187805. 
  33. ↑ "The receptor for the cytotoxic ligand TRAIL". Science 276 (5309): 111–113. April 1997. doi:10.1126/science.276.5309.111. PMID 9082980. 
  34. ↑ "TRUSS, a novel tumor necrosis factor receptor 1 scaffolding protein that mediates activation of the transcription factor NF-kappaB". Molecular and Cellular Biology 23 (22): 8334–8344. November 2003. doi:10.1128/MCB.23.22.8334-8344.2003. PMID 14585990. 
  35. ↑ "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology 6 (2): 97–105. February 2004. doi:10.1038/ncb1086. PMID 14743216. 
  36. ↑ "The TNF receptor 1: a split personality complex". Cell 114 (2): 148–150. July 2003. doi:10.1016/s0092-8674(03)00561-0. PMID 12887914. 
  37. ↑ "hUBC9 associates with MEKK1 and type I TNF-alpha receptor and stimulates NFkappaB activity". FEBS Letters 425 (3): 431–435. April 1998. doi:10.1016/S0014-5793(98)00287-7. PMID 9563508. Bibcode: 1998FEBSL.425..431S. 

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Template:TNF receptor superfamily modulators



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