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Tumor necrosis factor receptor superfamily, member 11a, NFKB activator
Identifiers
Symbols TNFRSF11A; CD265; ODFR; OFE; RANK; TRANCER
External IDs OMIM603499 MGI1314891 HomoloGene2848 GeneCards: TNFRSF11A Gene
RNA expression pattern
PBB GE TNFRSF11A 207037 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8792 21934
Ensembl ENSG00000141655 ENSMUSG00000026321
UniProt Q9Y6Q6 O35305
RefSeq (mRNA) NM_003839 NM_009399
RefSeq (protein) NP_003830 NP_033425
Location (UCSC) Chr 18:
58.14 - 58.21 Mb
Chr 1:
107.61 - 107.67 Mb
PubMed search [1] [2]

Receptor Activator of Nuclear Factor κ B (RANK), also known as TRANCE Receptor, is a type I membrane protein that is expressed on the surface of osteoclasts and is involved in their activation upon ligand binding. RANK is also expressed on dendritic cells and facilitates immune signaling. RANKL (Receptor Activator for Nuclear Factor κ B Ligand) is found on the surface of stromal cells, osteoblasts, and T cells.[1][2][3]

Contents

Interactions

RANK has been shown to interact with TRAF6,[4][5][6][7][8] TRAF5,[5][6][7] TRAF1,[7][8] TRAF2[5][6][7][8] and TRAF3.[7][8]

See also

References

  1. ^ Suda T, Takahashi N, Udagawa N, Jimi E, Gillespie MT, Martin TJ (1999). "Modulation of osteoclast differentiation and function by the new members of the tumor necrosis factor receptor and ligand families". Endocr. Rev. 20 (3): 345–57. doi:10.1210/er.20.3.345. PMID 10368775.  
  2. ^ Wong BR, Josien R, Choi Y (1999). "TRANCE is a TNF family member that regulates dendritic cell and osteoclast function". J. Leukoc. Biol. 65 (6): 715–24. PMID 10380891. http://www.jleukbio.org/cgi/content/abstract/65/6/715.  
  3. ^ Theill LE, Boyle WJ, Penninger JM (2002). "RANK-L and RANK: T cells, bone loss, and mammalian evolution". Annu. Rev. Immunol. 20: 795–823. doi:10.1146/annurev.immunol.20.100301.064753. PMID 11861618.  
  4. ^ Mizukami, Junko; Takaesu Giichi, Akatsuka Hiroyuki, Sakurai Hiroaki, Ninomiya-Tsuji Jun, Matsumoto Kunihiro, Sakurai Naoki (Feb. 2002). "Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6". Mol. Cell. Biol. (United States) 22 (4): 992–1000. ISSN 0270-7306. PMID 11809792.  
  5. ^ a b c Darnay, B G; Haridas V, Ni J, Moore P A, Aggarwal B B (Aug. 1998). "Characterization of the intracellular domain of receptor activator of NF-kappaB (RANK). Interaction with tumor necrosis factor receptor-associated factors and activation of NF-kappab and c-Jun N-terminal kinase". J. Biol. Chem. (UNITED STATES) 273 (32): 20551–5. ISSN 0021-9258. PMID 9685412.  
  6. ^ a b c Darnay, B G; Ni J, Moore P A, Aggarwal B B (Mar. 1999). "Activation of NF-kappaB by RANK requires tumor necrosis factor receptor-associated factor (TRAF) 6 and NF-kappaB-inducing kinase. Identification of a novel TRAF6 interaction motif". J. Biol. Chem. (UNITED STATES) 274 (12): 7724–31. ISSN 0021-9258. PMID 10075662.  
  7. ^ a b c d e Galibert, L; Tometsko M E, Anderson D M, Cosman D, Dougall W C (Dec. 1998). "The involvement of multiple tumor necrosis factor receptor (TNFR)-associated factors in the signaling mechanisms of receptor activator of NF-kappaB, a member of the TNFR superfamily". J. Biol. Chem. (UNITED STATES) 273 (51): 34120–7. ISSN 0021-9258. PMID 9852070.  
  8. ^ a b c d Kim, H H; Lee D E, Shin J N, Lee Y S, Jeon Y M, Chung C H, Ni J, Kwon B S, Lee Z H (Jan. 1999). "Receptor activator of NF-kappaB recruits multiple TRAF family adaptors and activates c-Jun N-terminal kinase". FEBS Lett. (NETHERLANDS) 443 (3): 297–302. ISSN 0014-5793. PMID 10025951.  

External links

Further reading

  • Romas E, Gillespie MT, Martin TJ (2002). "Involvement of receptor activator of NFkappaB ligand and tumor necrosis factor-alpha in bone destruction in rheumatoid arthritis.". Bone 30 (2): 340–6. doi:10.1016/S8756-3282(01)00682-2. PMID 11856640.  
  • Collin-Osdoby P (2005). "Regulation of vascular calcification by osteoclast regulatory factors RANKL and osteoprotegerin.". Circ. Res. 95 (11): 1046–57. doi:10.1161/01.RES.0000149165.99974.12. PMID 15564564.  
  • Clohisy DR, Mantyh PW (2005). "Bone cancer pain and the role of RANKL/OPG.". Journal of musculoskeletal & neuronal interactions 4 (3): 293–300. PMID 15615497.  
  • Anandarajah AP, Schwarz EM (2006). "Anti-RANKL therapy for inflammatory bone disorders: Mechanisms and potential clinical applications.". J. Cell. Biochem. 97 (2): 226–32. doi:10.1002/jcb.20674. PMID 16240334.  
  • Baud'huin M, Duplomb L, Ruiz Velasco C, et al. (2007). "Key roles of the OPG-RANK-RANKL system in bone oncology.". Expert Rev Anticancer Ther 7 (2): 221–32. doi:10.1586/14737140.7.2.221. PMID 17288531.  
  • Boyce BF, Xing L (2007). "Biology of RANK, RANKL, and osteoprotegerin.". Arthritis Res. Ther. 9 Suppl 1: S1. doi:10.1186/ar2165. PMID 17634140.  
  • Hughes AE, Shearman AM, Weber JL, et al. (1994). "Genetic linkage of familial expansile osteolysis to chromosome 18q.". Hum. Mol. Genet. 3 (2): 359–61. doi:10.1093/hmg/3.2.359. PMID 7911698.  
  • Cody JD, Singer FR, Roodman GD, et al. (1997). "Genetic linkage of Paget disease of the bone to chromosome 18q.". Am. J. Hum. Genet. 61 (5): 1117–22. doi:10.1086/301601. PMID 9345096.  
  • Anderson DM, Maraskovsky E, Billingsley WL, et al. (1997). "A homologue of the TNF receptor and its ligand enhance T-cell growth and dendritic-cell function.". Nature 390 (6656): 175–9. doi:10.1038/36593. PMID 9367155.  
  • Haslam SI, Van Hul W, Morales-Piga A, et al. (1998). "Paget's disease of bone: evidence for a susceptibility locus on chromosome 18q and for genetic heterogeneity.". J. Bone Miner. Res. 13 (6): 911–7. doi:10.1359/jbmr.1998.13.6.911. PMID 9626621.  
  • Darnay BG, Haridas V, Ni J, et al. (1998). "Characterization of the intracellular domain of receptor activator of NF-kappaB (RANK). Interaction with tumor necrosis factor receptor-associated factors and activation of NF-kappab and c-Jun N-terminal kinase.". J. Biol. Chem. 273 (32): 20551–5. doi:10.1074/jbc.273.32.20551. PMID 9685412.  
  • Wong BR, Josien R, Lee SY, et al. (1998). "The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor.". J. Biol. Chem. 273 (43): 28355–9. doi:10.1074/jbc.273.43.28355. PMID 9774460.  
  • Galibert L, Tometsko ME, Anderson DM, et al. (1999). "The involvement of multiple tumor necrosis factor receptor (TNFR)-associated factors in the signaling mechanisms of receptor activator of NF-kappaB, a member of the TNFR superfamily.". J. Biol. Chem. 273 (51): 34120–7. doi:10.1074/jbc.273.51.34120. PMID 9852070.  
  • Nakagawa N, Kinosaki M, Yamaguchi K, et al. (1999). "RANK is the essential signaling receptor for osteoclast differentiation factor in osteoclastogenesis.". Biochem. Biophys. Res. Commun. 253 (2): 395–400. doi:10.1006/bbrc.1998.9788. PMID 9878548.  
  • Kim HH, Lee DE, Shin JN, et al. (1999). "Receptor activator of NF-kappaB recruits multiple TRAF family adaptors and activates c-Jun N-terminal kinase.". FEBS Lett. 443 (3): 297–302. doi:10.1016/S0014-5793(98)01731-1. PMID 10025951.  
  • Darnay BG, Ni J, Moore PA, Aggarwal BB (1999). "Activation of NF-kappaB by RANK requires tumor necrosis factor receptor-associated factor (TRAF) 6 and NF-kappaB-inducing kinase. Identification of a novel TRAF6 interaction motif.". J. Biol. Chem. 274 (12): 7724–31. doi:10.1074/jbc.274.12.7724. PMID 10075662.  
  • Hsu H, Lacey DL, Dunstan CR, et al. (1999). "Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand.". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3540–5. doi:10.1073/pnas.96.7.3540. PMID 10097072.  
  • Dougall WC, Glaccum M, Charrier K, et al. (1999). "RANK is essential for osteoclast and lymph node development.". Genes Dev. 13 (18): 2412–24. doi:10.1101/gad.13.18.2412. PMID 10500098.  
  • Hughes AE, Ralston SH, Marken J, et al. (2000). "Mutations in TNFRSF11A, affecting the signal peptide of RANK, cause familial expansile osteolysis.". Nat. Genet. 24 (1): 45–8. doi:10.1038/71667. PMID 10615125.  
  • Wong BR, Besser D, Kim N, et al. (2000). "TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src.". Mol. Cell 4 (6): 1041–9. doi:10.1016/S1097-2765(00)80232-4. PMID 10635328.  

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








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