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]
Quick Facts TNFRSF1A, Available structures ...
TNFRSF1A |
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Identifiers |
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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 |
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External IDs | OMIM: 191190; MGI: 1314884; HomoloGene: 828; GeneCards: TNFRSF1A; OMA:TNFRSF1A - orthologs |
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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]
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]
TNFRSF1A has been shown to interact with:
- BAG4,[15][16]
- CASP10,[17][18]
- FADD,[17][19]
- IKK2,[20][21]
- JAK1,[22][23]
- JAK2,[22]
- PIP4K2B,[24]
- PSMD2,[25][26]
- RIPK1,[27][28][29][30][31][32]
- SUMO1,[33][34]
- TRADD[15][19][27][30][35][36][37]
- TRAF2,[19][27][35]
- TRPC4AP,[38]
- TNF,[39][40] and
- UBE2I.[41]
Baker E, Chen LZ, Smith CA, Callen DF, Goodwin R, Sutherland GR (November 1991). "Chromosomal location of the human tumor necrosis factor receptor genes". Cytogenetics and Cell Genetics. 57 (2–3): 117–118. doi:10.1159/000133127. PMID 1655358.
Hope S, Melle I, Aukrust P, Steen NE, Birkenaes AB, Lorentzen S, et al. (November 2009). "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. doi:10.1111/j.1399-5618.2009.00757.x. hdl:10852/34620. PMID 19839997.
Buchhave P, Zetterberg H, Blennow K, Minthon L, Janciauskiene S, Hansson O (November 2010). "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. doi:10.1016/j.neurobiolaging.2008.10.012. PMID 19070941. S2CID 34595960.
Diniz BS, Teixeira AL, Ojopi EB, Talib LL, Mendonça VA, Gattaz WF, et al. (2010). "Higher serum sTNFR1 level predicts conversion from mild cognitive impairment to Alzheimer's disease". Journal of Alzheimer's Disease. 22 (4): 1305–1311. doi:10.3233/JAD-2010-100921. PMID 20930310.
Miscia S, Marchisio M, Grilli A, Di Valerio V, Centurione L, Sabatino G, et al. (January 2002). "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. PMID 11801527.
Blankenship JW, Varfolomeev E, Goncharov T, Fedorova AV, Kirkpatrick DS, Izrael-Tomasevic A, et al. (January 2009). "Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2(1)". The Biochemical Journal. 417 (1): 149–160. doi:10.1042/BJ20081885. PMID 18939944.
Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, et al. (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.