NRIP1

NRIP1
Nuclear receptor interacting protein 1

Rendering of 2GPO
Identifiers
Symbols NRIP1; FLJ77253; RIP140
External IDs OMIM: 602490 MGI: 1315213 HomoloGene: 2606 GeneCards: NRIP1 Gene
RNA expression pattern
PBB GE NRIP1 202600 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8204 268903
Ensembl ENSG00000180530 ENSMUSG00000048490
UniProt P48552 Q3U166
RefSeq (mRNA) NM_003489.3 NM_173440.2
RefSeq (protein) NP_003480.2 NP_775616.1
Location (UCSC) Chr 21:
16.33 – 16.44 Mb		 Chr 16:
76.29 – 76.37 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 is a key regulator which modulates transcriptional activity of a variety of transcription factors, including the estrogen receptor.[3]

RIP140 has an important role in regulating lipid and glucose metabolism,[4] and regulates gene expression in metabolic tissues including heart,[5] skeletal muscle,[6] and liver.[7]

Knockout mice that completely lack the RIP140 molecule are lean and stay lean, even on a rich diet.[8] RIP140 is part of the chain by which tumors can cause cachexia.[9][10]

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.[11]

Estrogen-related receptor alpha (ERRa) can activate RIP140 during adipogenesis, by means of directly binding to an estrogen receptor element/ERR element and indirectly through Sp1 binding to the proximal promoter. [12]

RIP140 suppresses the expression of mitochondrial proteins succinate dehydrogenase complex b and CoxVb and acts as a negative regulator of glucose uptake in mice. [13]


Knockout mice (females) are also infertile because they fail to ovulate.[14] Failure of ovulation in these mice is caused by lack of cumulus expansion and altered expression of various genes, including amphiregulin, in ovarian follicles.[15] [16]

Levels of RIP140 expression in various tissues varies during aging in mice, suggesting changes in metabolic function.[17] RIP140 is implicated in certain human disease processes. In morbid obesity, RIP140 levels are down-regulated in visceral adipose tissue.[18] In breast cancer, RIP140 is involved in regulation of E2F1, an oncogene which discriminates between luminal and basal types of tumours. RIP140 has an influence upon cancer phenotype and prognosis.[19] In addition, RIP140 has a role in inflammation, since it acts as a coactivator for NFkappaB/RelA-dependent cytokine gene expression. Lack of RIP140 leads to an inhibition of proinflammatory pathways in macrophages.[20]

Contents

Interactions

NRIP1 has been shown to interact with Retinoic acid receptor alpha,[21][22][23] YWHAQ,[24] Glucocorticoid receptor,[24][25][26] Histone deacetylase 5,[27] CTBP2,[27][28] Estrogen receptor alpha,[1][23][29] Aryl hydrocarbon receptor,[30] Steroidogenic factor 1,[31][32] DAX1,[32] CTBP1[27][33] and Retinoid X receptor alpha.[22][23]

See also

References

  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. PMC 394449. PMID 7641693. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=394449. 
  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. doi:10.1007/s004390050682. PMID 9521594. 
  3. ^ "Entrez Gene: NRIP1 nuclear receptor interacting protein 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8204. 
  4. ^ Rosell M, Jones MC, Parker MG (2010). "Role of nuclear receptor corepressor RIP140 in metabolic syndrome.". Biochim Biophys Acta. doi:10.1016/j.bbadis.2010.12.106. PMID 21193034. 
  5. ^ Fritah A, Steel JH, Nichol D, Parker N, Williams S, Price A, Strauss L, Ryder TA, Mobberley MA, Poutanen M, Parker M, White R (2010). "Elevated expression of the metabolic regulator receptor-interacting protein 140 results in cardiac hypertrophy and impaired cardiac function.". Cardiovasc Res 86 (3): 443–451. doi:10.1093/cvr/cvp418. PMC 2868176. PMID 20083575. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2868176. 
  6. ^ Seth A, Steel JH, Nichol D, Pocock V, Kumaran MK, Fritah A, Mobberley M, Ryder TA, Rowlerson A, Scott J, Poutanen M, White R, Parker M. (Sep 2007). "The transcriptional corepressor RIP140 regulates oxidative metabolism in skeletal muscle". Cell Metab 6 (3): 236–245. doi:10.1016/j.cmet.2007.08.004. PMC 2680991. PMID 17767910. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2680991. 
  7. ^ Herzog B, Hallberg M, Seth A, Woods A, White R, Parker MG. (Nov 2007). "The nuclear receptor cofactor, receptor-interacting protein 140, is required for the regulation of hepatic lipid and glucose metabolism by liver X receptor". Mol Endocrionol 21 (11): 2687–97. doi:10.1210/me.2007-1213. PMC 2140279. PMID 17684114. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2140279. 
  8. ^ Leonardsson G, Steel JH, Christian M, Pocock V, Milligan S, Bell J, So PW, Medina-Gomez G, Vidal-Puig A, White R, Parker MG (May 2004). "Nuclear receptor corepressor RIP140 regulates fat accumulation". Proc Natl Acad Sci U S A 101 (22): 8437–42. doi:10.1073/pnas.0401013101. PMC 420412. PMID 15155905. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=420412. 
  9. ^ "A common denominator of inflammations and fatty liver". News. Science Centric. 2008-05-31. http://www.sciencecentric.com/news/article.php?q=08052824. Retrieved 2008-08-31. [dead link]
  10. ^ 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. 
  11. ^ 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. PMC 2072047. PMID 17456798. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2072047. 
  12. ^ Nichol D, Christian M, Steel JH, White R, Parker MG. (Oct 2006). "RIP140 expression is stimulated by estrogen-related receptor alpha during adipogenesis.". J Biol Chem 281 (43): 32140–32147. doi:10.1074/jbc.M604803200. PMID 16923809. 
  13. ^ Powelka AM, Seth A, Virbasius JV, Kiskinis E, Nicoloro SM, Guilherme A, Tang X, Straubhaar J, Cherniack AD, Parker MG, Czech MP. (2006). "Suppression of oxidative metabolism and mitochondrial biogenesis by the transcriptional corepressor RIP140 in mouse adipocytes.". J Clin Invest 116 (1): 125–136. doi:10.1172/JCI26040. PMID 16374519. 
  14. ^ White R, Leonardsson G, Rosewell I, Ann Jacobs M, Milligan S, Parker M. (Dec 2000). "The nuclear receptor co-repressor nrip1 (RIP140) is essential for female fertility". Nat. Med. 6 (12): 1368–74. doi:10.1038/82183. PMID 11100122. 
  15. ^ Tullet JMA, Pocock V, Steel JH, White R, Milligan S and Parker MG (2005). "Multiple Signaling Defects in the Absence of RIP140 Impair Both Cumulus Expansion and Follicle Rupture". Endocrinology 146 (9): 4127–4137. doi:10.1210/en.+2005-0348. PMID 15919748. 
  16. ^ Nautiyal J, Steel JH, Rosell MM, Nikolopoulou E, Lee K, Demayo FJ, White R, Richards JS, Parker MG (2010). "The nuclear receptor cofactor receptor-interacting protein 140 is a positive regulator of amphiregulin expression and cumulus cell-oocyte complex expansion in the mouse ovary". Endocrinology 151 (6): 2923–2932. doi:10.1210/en.+2010-0081. PMC 2875814. PMID 20308529. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2875814. 
  17. ^ Ghosh S, Thakur MK. (2008). "Tissue-specific expression of receptor-interacting protein in aging mouse". Age (Dordr) 30 (4): 237–243. doi:10.1007/s11357-008-9062-3. PMC 2585652. PMID 19424847. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2585652. 
  18. ^ Catalán V, Gómez-Ambrosi J, Lizanzu A, Rodríguez A, Silva C, Rotellar F, Gil MJ, Cienfuegos JA, Salvador J, Frühbeck G (2009). "RIP140 gene and protein expression levels are downregulated in visceral adipose tissue in human morbid obesity". Obse Surg 19 (6): 771–776. doi:10.1007/s11695-009-9834-6. PMID 19367438. 
  19. ^ Docquier A, Harmand PO, Fritsch S, Chanrion M, Darbon JM, Cavaillès V. (2010). "The transcriptional coregulator RIP140 represses E2F1 activity and discriminates breast cancer subtypes". Clin Cancer Res 16 (11): 2959–2970. doi:10.1158/1078-0432.CCR-09-3153. PMID 20410059. 
  20. ^ Zschiedrich I, Hardeland U, Krones-Herzig A, Berriel Diaz M, Vegiopoulos A, Müggenburg J, Sombroek D, Hofmann TG, Zawatzky R, Yu X, Gretz N, Christian M, White R, Parker MG, Herzig S (2008). "Coactivator function of RIP140 for NFkappaB/RelA-dependent cytokine gene expression". Blood 112 (2): 264–276. doi:10.1182/blood-2007-11-121699. PMID 18469200. 
  21. ^ 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. 
  22. ^ 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. 
  23. ^ 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. PMC 231605. PMID 8887632. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231605. 
  24. ^ 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. doi:10.1210/me.15.4.501. ISSN 0888-8809. PMID 11266503. 
  25. ^ 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. doi:10.1128/MCB.23.12.4187-4198.2003. ISSN 0270-7306. PMC 156128. PMID 12773562. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=156128. 
  26. ^ 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. doi:10.1074/jbc.274.25.18121. ISSN 0021-9258. PMID 10364267. 
  27. ^ 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. PMC 390375. PMID 15060175. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=390375. 
  28. ^ 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. 
  29. ^ 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. doi:10.1074/jbc.272.18.12062. ISSN 0021-9258. PMID 9115274. 
  30. ^ 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. doi:10.1074/jbc.274.32.22155. ISSN 0021-9258. PMID 10428779. 
  31. ^ 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. doi:10.1016/S0303-7207(03)00097-2. ISSN 0303-7207. PMID 12782406. 
  32. ^ 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. doi:10.1210/en.142.8.3570. ISSN 0013-7227. PMID 11459805. 
  33. ^ 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. PMC 2364611. PMID 18374649. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2364611. 

External links

Further reading

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

v · d · eTranscription coregulators
Coactivators
ARA (54, 55, 70) • BCAS3 • CARM1 • p300-CBP (EP300, CREBBP) • CRTC (1, 2, 3) • DRIP/TRAP • MN1 • PCAF • PNRC (1, 2) • PPARGC (1A, 1B) • TGFB1I1
NCOA1 (SRC-1) • NCOA2 (GRIP1/SRC-2/TIF2) • NCOA3 (AIB/SRC-3/TRAM-1) • NCOA4 (ARA70) • NCOA5 (CIA) • NCOA6 (RAP250) • NCOA7 (ERAP140)
Corepressors
CTBP (1, 2) • Hairless homolog • LCOR • NRIP1 (RIP140) • PELP-1 • RCOR1 • Rb • SIN3A • SIN3B • Tripartite motif family TRIM (24, 28, 33)
NCOR1 • NCOR2 (SMRT)
ATP-dependent remodeling factors
see also transcription factor/coregulator deficiencies
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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