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Nuclear receptor interacting protein 1
Symbols NRIP1; RIP140
External IDs OMIM602490 MGI1315213 HomoloGene2606 GeneCards: NRIP1 Gene
RNA expression pattern
PBB GE NRIP1 202600 s at tn.png
More reference expression data
Species Human Mouse
Entrez 8204 268903
Ensembl ENSG00000180530 ENSMUSG00000048490
UniProt P48552 Q3U166
RefSeq (mRNA) NM_003489 NM_173440
RefSeq (protein) NP_003480 NP_775616
Location (UCSC) Chr 21:
15.26 - 15.26 Mb
Chr 16:
76.17 - 76.26 Mb
PubMed search [1] [2]

Nuclear receptor-interacting protein 1 is a protein that in humans is encoded by the NRIP1 gene.[1][2]

Nuclear receptor interacting protein 1 (NRIP1) is a nuclear protein that specifically interacts with the hormone-dependent activation domain AF2 of nuclear receptors. Also known as RIP140, this protein modulates transcriptional activity of the estrogen receptor.[3]

Knockout mice that completely lack the RIP140 molecule are lean and stay lean, even on a rich diet. RIP140 is part of the chain by which tumors can cause cachexia. [4][5]

A major role for RIP140 in adipose tissue is to block the expression of genes involved in energy dissipation and mitochondrial uncoupling, including uncoupling protein 1 and carnitine palmitoyltransferase 1b.[6]



NRIP1 has been shown to interact with Retinoic acid receptor alpha,[7][8][9] YWHAQ,[10] Glucocorticoid receptor,[11][10][12] Histone deacetylase 5,[13] CTBP2,[14][13] Estrogen receptor alpha,[1][15][9] Aryl hydrocarbon receptor,[16] Steroidogenic factor 1,[17][18] DAX1,[18] CTBP1[13][19] and Retinoid X receptor alpha.[8][9]

See also

External links


  1. ^ a b Cavailles V, Dauvois S, L'Horset F, Lopez G, Hoare S, Kushner PJ, Parker MG (Sep 1995). "Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor". EMBO J 14 (15): 3741–51. PMID 7641693.  
  2. ^ Katsanis N, Ives JH, Groet J, Nizetic D, Fisher EM (Apr 1998). "Localisation of receptor interacting protein 140 (RIP140) within 100 kb of D21S13 on 21q11, a gene-poor region of the human genome". Hum Genet 102 (2): 221–3. PMID 9521594.  
  3. ^ "Entrez Gene: NRIP1 nuclear receptor interacting protein 1".  
  4. ^ "A common denominator of inflammations and fatty liver". News. Science Centric. 2008-05-31. Retrieved 2008-08-31.  
  5. ^ Diaz MB, Krones-Herzig A, Metzger D, Ziegler A, Vegiopoulos A, Klingenspor M, Müller-Decker K, Herzig S (April 2008). "Nuclear receptor cofactor receptor interacting protein 140 controls hepatic triglyceride metabolism during wasting in mice". Hepatology 48 (3): 782–791. doi:10.1002/hep.22383. PMID 18712775.  
  6. ^ Debevec D, Christian M, Morganstein D, Seth A, Herzog B, Parker M, White R (July 2007). "Receptor interacting protein 140 regulates expression of uncoupling protein 1 in adipocytes through specific peroxisome proliferator activated receptor isoforms and estrogen-related receptor alpha". Mol. Endocrinol. 21 (7): 1581–92. doi:10.1210/me.2007-0103. PMID 17456798.  
  7. ^ Hu, Xinli; Chen Yixin, Farooqui Mariya, Thomas Mary C, Chiang Cheng-Ming, Wei Li-Na (Jan. 2004). "Suppressive effect of receptor-interacting protein 140 on coregulator binding to retinoic acid receptor complexes, histone-modifying enzyme activity, and gene activation". J. Biol. Chem. (United States) 279 (1): 319–25. doi:10.1074/jbc.M307621200. ISSN 0021-9258. PMID 14581481.  
  8. ^ a b Farooqui, Mariya; Franco Peter J, Thompson Jim, Kagechika Hiroyuki, Chandraratna Roshantha A S, Banaszak Len, Wei Li-Na (Feb. 2003). "Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity". Biochemistry (United States) 42 (4): 971–9. doi:10.1021/bi020497k. ISSN 0006-2960. PMID 12549917.  
  9. ^ a b c L'Horset, F; Dauvois S, Heery D M, Cavaillès V, Parker M G (Nov. 1996). "RIP-140 interacts with multiple nuclear receptors by means of two distinct sites". Mol. Cell. Biol. (UNITED STATES) 16 (11): 6029–36. ISSN 0270-7306. PMID 8887632.  
  10. ^ a b Zilliacus, J; Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson J A (Apr. 2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140". Mol. Endocrinol. (United States) 15 (4): 501–11. ISSN 0888-8809. PMID 11266503.  
  11. ^ Tazawa, Hiroshi; Osman Waffa, Shoji Yutaka, Treuter Eckardt, Gustafsson Jan-Ake, Zilliacus Johanna (Jun. 2003). "Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140". Mol. Cell. Biol. (United States) 23 (12): 4187–98. ISSN 0270-7306. PMID 12773562.  
  12. ^ Subramaniam, N; Treuter E, Okret S (Jun. 1999). "Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids". J. Biol. Chem. (UNITED STATES) 274 (25): 18121–7. ISSN 0021-9258. PMID 10364267.  
  13. ^ a b c Castet, Audrey; Boulahtouf Abdelhay, Versini Gwennaëlle, Bonnet Sandrine, Augereau Patrick, Vignon Françoise, Khochbin Saadi, Jalaguier Stéphan, Cavaillès Vincent (2004). "Multiple domains of the Receptor-Interacting Protein 140 contribute to transcription inhibition". Nucleic Acids Res. (England) 32 (6): 1957–66. doi:10.1093/nar/gkh524. PMID 15060175.  
  14. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.  
  15. ^ Thénot, S; Henriquet C, Rochefort H, Cavaillès V (May. 1997). "Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1". J. Biol. Chem. (UNITED STATES) 272 (18): 12062–8. ISSN 0021-9258. PMID 9115274.  
  16. ^ Kumar, M B; Tarpey R W, Perdew G H (Aug. 1999). "Differential recruitment of coactivator RIP140 by Ah and estrogen receptors. Absence of a role for LXXLL motifs". J. Biol. Chem. (UNITED STATES) 274 (32): 22155–64. ISSN 0021-9258. PMID 10428779.  
  17. ^ Mellgren, Gunnar; Børud Bente, Hoang Tuyen, Yri Olav Erich, Fladeby Cathrine, Lien Ernst Asbjørn, Lund Johan (May. 2003). "Characterization of receptor-interacting protein RIP140 in the regulation of SF-1 responsive target genes". Mol. Cell. Endocrinol. (Ireland) 203 (1-2): 91–103. ISSN 0303-7207. PMID 12782406.  
  18. ^ a b Sugawara, T; Abe S, Sakuragi N, Fujimoto Y, Nomura E, Fujieda K, Saito M, Fujimoto S (Aug. 2001). "RIP 140 modulates transcription of the steroidogenic acute regulatory protein gene through interactions with both SF-1 and DAX-1". Endocrinology (United States) 142 (8): 3570–7. ISSN 0013-7227. PMID 11459805.  
  19. ^ Perissi, Valentina; Scafoglio Claudio, Zhang Jie, Ohgi Kenneth A, Rose David W, Glass Christopher K, Rosenfeld Michael G (Mar. 2008). "TBL1 and TBLR1 phosphorylation on regulated gene promoters overcomes dual CtBP and NCoR/SMRT transcriptional repression checkpoints". Mol. Cell (United States) 29 (6): 755–66. doi:10.1016/j.molcel.2008.01.020. PMID 18374649.  

Further reading

  • Detlav IE (1976). "[Anti-brain antibodies in serum and cerebrospinal fluid following cranio-cerebral trauma]". Zhurnal nevropatologii i psikhiatrii imeni S.S. Korsakova (Moscow, Russia : 1952) 76 (3): 344–8. PMID 1266503.  
  • L'Horset F, Dauvois S, Heery DM, et al. (1996). "RIP-140 interacts with multiple nuclear receptors by means of two distinct sites.". Mol. Cell. Biol. 16 (11): 6029–36. PMID 8887632.  
  • Yan ZH, Karam WG, Staudinger JL, et al. (1998). "Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4.". J. Biol. Chem. 273 (18): 10948–57. doi:10.1074/jbc.273.18.10948. PMID 9556573.  
  • Treuter E, Albrektsen T, Johansson L, et al. (1998). "A regulatory role for RIP140 in nuclear receptor activation.". Mol. Endocrinol. 12 (6): 864–81. doi:10.1210/me.12.6.864. PMID 9626662.  
  • Eng FC, Barsalou A, Akutsu N, et al. (1998). "Different classes of coactivators recognize distinct but overlapping binding sites on the estrogen receptor ligand binding domain.". J. Biol. Chem. 273 (43): 28371–7. doi:10.1074/jbc.273.43.28371. PMID 9774463.  
  • Lee CH, Chinpaisal C, Wei LN (1998). "Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2.". Mol. Cell. Biol. 18 (11): 6745–55. PMID 9774688.  
  • Miyata KS, McCaw SE, Meertens LM, et al. (1999). "Receptor-interacting protein 140 interacts with and inhibits transactivation by, peroxisome proliferator-activated receptor alpha and liver-X-receptor alpha.". Mol. Cell. Endocrinol. 146 (1-2): 69–76. doi:10.1016/S0303-7207(98)00196-8. PMID 10022764.  
  • Subramaniam N, Treuter E, Okret S (1999). "Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids.". J. Biol. Chem. 274 (25): 18121–7. doi:10.1074/jbc.274.25.18121. PMID 10364267.  
  • Wiebel FF, Steffensen KR, Treuter E, et al. (1999). "Ligand-independent coregulator recruitment by the triply activatable OR1/retinoid X receptor-alpha nuclear receptor heterodimer.". Mol. Endocrinol. 13 (7): 1105–18. doi:10.1210/me.13.7.1105. PMID 10406462.  
  • Kumar MB, Tarpey RW, Perdew GH (1999). "Differential recruitment of coactivator RIP140 by Ah and estrogen receptors. Absence of a role for LXXLL motifs.". J. Biol. Chem. 274 (32): 22155–64. doi:10.1074/jbc.274.32.22155. PMID 10428779.  
  • Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21.". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.  
  • Wei LN, Hu X, Chandra D, et al. (2001). "Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing.". J. Biol. Chem. 275 (52): 40782–7. doi:10.1074/jbc.M004821200. PMID 11006275.  
  • Zilliacus J, Holter E, Wakui H, et al. (2001). "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140.". Mol. Endocrinol. 15 (4): 501–11. doi:10.1210/me.15.4.501. PMID 11266503.  
  • Mal A, Sturniolo M, Schiltz RL, et al. (2001). "A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program.". Embo J. 20 (7): 1739–53. doi:10.1093/emboj/20.7.1739. PMID 11285237.  
  • Sugawara T, Abe S, Sakuragi N, et al. (2001). "RIP 140 modulates transcription of the steroidogenic acute regulatory protein gene through interactions with both SF-1 and DAX-1.". Endocrinology 142 (8): 3570–7. doi:10.1210/en.142.8.3570. PMID 11459805.  
  • Vo N, Fjeld C, Goodman RH (2001). "Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP.". Mol. Cell. Biol. 21 (18): 6181–8. doi:10.1128/MCB.21.18.6181-6188.2001. PMID 11509661.  
  • Zennaro MC, Souque A, Viengchareun S, et al. (2002). "A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action.". Mol. Endocrinol. 15 (9): 1586–98. doi:10.1210/me.15.9.1586. PMID 11518808.  
  • Chen Y, Kerimo A, Khan S, Wei LN (2003). "Real-time analysis of molecular interaction of retinoid receptors and receptor-interacting protein 140 (RIP140).". Mol. Endocrinol. 16 (11): 2528–37. doi:10.1210/me.2002-0124. PMID 12403842.  

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



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