NRIP1

Last updated
NRIP1
PDB 2gpo EBI.jpg
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases NRIP1 , RIP140, nuclear receptor interacting protein 1, CAKUT3
External IDs OMIM: 602490 MGI: 1315213 HomoloGene: 2606 GeneCards: NRIP1
Orthologs
SpeciesHumanMouse
Entrez

8204

268903

Ensembl

ENSG00000180530

ENSMUSG00000048490

UniProt

P48552

Q8CBD1

RefSeq (mRNA)

NM_003489

NM_173440
NM_001358238

RefSeq (protein)

NP_003480

NP_775616
NP_001345167

Location (UCSC) Chr 21: 14.96 – 15.07 Mb Chr 16: 76.08 – 76.17 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
Nuclear receptor-interacting protein 1 repression 1
Identifiers
SymbolNRIP1_repr_1
Pfam PF15687
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Nuclear receptor-interacting protein 1 repression 2
Identifiers
SymbolNRIP1_repr_2
Pfam PF15688
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Nuclear receptor-interacting protein 1 repression 3
Identifiers
SymbolNRIP1_repr_3
Pfam PF15689
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Nuclear receptor-interacting protein 1 repression 4
Identifiers
SymbolNRIP1_repr_4
Pfam PF15690
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Nuclear receptor-interacting protein 1 (NRIP1) also known as receptor-interacting protein 140 (RIP140) is a protein that in humans is encoded by the NRIP1 gene. [5] [6]

Contents

Function

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. [7]

RIP140 has an important role in regulating lipid and glucose metabolism, [8] and regulates gene expression in metabolic tissues including heart, [9] skeletal muscle, [10] and liver. [11] 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. [12]

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. [13]

RIP140 suppresses the expression of mitochondrial proteins succinate dehydrogenase complex b and CoxVb and acts as a negative regulator of glucose uptake in mice. [14]

Knockout studies

Knockout mice that completely lack the RIP140 molecule are lean and stay lean, even on a rich diet. [15]

Knockout mice (females) are also infertile because they fail to ovulate. [16] Failure of ovulation in these mice is caused by lack of cumulus expansion and altered expression of various genes, including amphiregulin, in ovarian follicles. [17] [18]

Clinical significance

RIP140 is part of the chain by which tumors can cause cachexia. [19] [20]

Levels of RIP140 expression in various tissues varies during aging in mice, suggesting changes in metabolic function. [21] RIP140 is implicated in certain human disease processes. In morbid obesity, RIP140 levels are down-regulated in visceral adipose tissue. [22] 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. [23] 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. [24]

Interactions

NRIP1 has been shown to interact with:

See also

Related Research Articles

In molecular biology and genetics, transcription coregulators are proteins that interact with transcription factors to either activate or repress the transcription of specific genes. Transcription coregulators that activate gene transcription are referred to as coactivators while those that repress are known as corepressors. The mechanism of action of transcription coregulators is to modify chromatin structure and thereby make the associated DNA more or less accessible to transcription. In humans several dozen to several hundred coregulators are known, depending on the level of confidence with which the characterisation of a protein as a coregulator can be made. One class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP dependent class modifies the conformation of chromatin.

<span class="mw-page-title-main">Mothers against decapentaplegic homolog 2</span> Protein-coding gene in the species Homo sapiens

Mothers against decapentaplegic homolog 2 also known as SMAD family member 2 or SMAD2 is a protein that in humans is encoded by the SMAD2 gene. MAD homolog 2 belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways.

<span class="mw-page-title-main">Nuclear receptor coactivator 1</span> Protein-coding gene in the species Homo sapiens

The nuclear receptor coactivator 1 (NCOA1) is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity. NCOA1 is recruited to DNA promotion sites by ligand-activated nuclear receptors. NCOA1, in turn, acylates histones, which makes downstream DNA more accessible to transcription. Hence, NCOA1 assists nuclear receptors in the upregulation of DNA expression.

<span class="mw-page-title-main">Nuclear receptor coactivator 2</span> Protein-coding gene in the species Homo sapiens

The nuclear receptor coactivator 2 also known as NCoA-2 is a protein that in humans is encoded by the NCOA2 gene. NCoA-2 is also frequently called glucocorticoid receptor-interacting protein 1 (GRIP1), steroid receptor coactivator-2 (SRC-2), or transcriptional mediators/intermediary factor 2 (TIF2).

<span class="mw-page-title-main">Nuclear receptor coactivator 3</span> Protein-coding gene in the species Homo sapiens

The nuclear receptor coactivator 3 also known as NCOA3 is a protein that, in humans, is encoded by the NCOA3 gene. NCOA3 is also frequently called 'amplified in breast 1' (AIB1), steroid receptor coactivator-3 (SRC-3), or thyroid hormone receptor activator molecule 1 (TRAM-1).

<span class="mw-page-title-main">Nuclear receptor co-repressor 1</span> Protein-coding gene in the species Homo sapiens

The nuclear receptor co-repressor 1 also known as thyroid-hormone- and retinoic-acid-receptor-associated co-repressor 1 (TRAC-1) is a protein that in humans is encoded by the NCOR1 gene.

<span class="mw-page-title-main">Small heterodimer partner</span> Protein-coding gene in the species Homo sapiens

The small heterodimer partner (SHP) also known as NR0B2 is a protein that in humans is encoded by the NR0B2 gene. SHP is a member of the nuclear receptor family of intracellular transcription factors. SHP is unusual for a nuclear receptor in that it lacks a DNA binding domain. Therefore, it is technically neither a transcription factor nor nuclear receptor but nevertheless it is still classified as such due to relatively high sequence homology with other nuclear receptor family members.

<span class="mw-page-title-main">Retinoid X receptor alpha</span> Protein-coding gene in the species Homo sapiens

Retinoid X receptor alpha (RXR-alpha), also known as NR2B1 is a nuclear receptor that in humans is encoded by the RXRA gene.

<span class="mw-page-title-main">Peroxisome proliferator-activated receptor alpha</span> Nuclear receptor protein found in humans

Peroxisome proliferator-activated receptor alpha (PPAR-α), also known as NR1C1, is a nuclear receptor protein functioning as a transcription factor that in humans is encoded by the PPARA gene. Together with peroxisome proliferator-activated receptor delta and peroxisome proliferator-activated receptor gamma, PPAR-alpha is part of the subfamily of peroxisome proliferator-activated receptors. It was the first member of the PPAR family to be cloned in 1990 by Stephen Green and has been identified as the nuclear receptor for a diverse class of rodent hepatocarcinogens that causes proliferation of peroxisomes.

<span class="mw-page-title-main">Thyroid hormone receptor beta</span> Protein-coding gene in the species Homo sapiens

Thyroid hormone receptor beta (TR-beta) also known as nuclear receptor subfamily 1, group A, member 2 (NR1A2), is a nuclear receptor protein that in humans is encoded by the THRB gene.

<span class="mw-page-title-main">MED1</span> Protein-coding gene in the species Homo sapiens

Mediator of RNA polymerase II transcription subunit 1 also known as DRIP205 or Trap220 is a subunit of the Mediator complex and is a protein that in humans is encoded by the MED1 gene. MED1 functions as a nuclear receptor coactivator.

<span class="mw-page-title-main">PIAS1</span> Protein-coding gene in the species Homo sapiens

E3 SUMO-protein ligase PIAS1 is an enzyme that in humans is encoded by the PIAS1 gene.

<span class="mw-page-title-main">SAFB</span> Protein-coding gene in the species Homo sapiens

Scaffold attachment factor B, also known as SAFB, is a gene with homologs that have been studied in humans and mice.

<span class="mw-page-title-main">AH receptor-interacting protein</span> Protein-coding gene in the species Homo sapiens

AH receptor-interacting protein (AIP) also known as aryl hydrocarbon receptor-interacting protein, immunophilin homolog ARA9, or HBV X-associated protein 2 (XAP-2) is a protein that in humans is encoded by the AIP gene. The protein is a member of the FKBP family.

<span class="mw-page-title-main">NCOA6</span> Protein-coding gene in the species Homo sapiens

Nuclear receptor coactivator 6 is a protein that in humans is encoded by the NCOA6 gene.

<span class="mw-page-title-main">MED14</span> Protein-coding gene in humans

Mediator of RNA polymerase II transcription subunit 14 is an enzyme that in humans is encoded by the MED14 gene.

<span class="mw-page-title-main">TRIM24</span> Protein-coding gene in the species Homo sapiens

Tripartite motif-containing 24 (TRIM24) also known as transcriptional intermediary factor 1α (TIF1α) is a protein that, in humans, is encoded by the TRIM24 gene.

<span class="mw-page-title-main">PCK1</span> Protein-coding gene in the species Homo sapiens

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<i>NFIC</i> (gene) Protein-coding gene in the species Homo sapiens

Nuclear factor 1 C-type is a protein that in humans is encoded by the NFIC gene.

Nuclear receptor coregulators are a class of transcription coregulators that have been shown to be involved in any aspect of signaling by any member of the nuclear receptor superfamily. A comprehensive database of coregulators for nuclear receptors and other transcription factors was previously maintained at the Nuclear Receptor Signaling Atlas website which has since been replaced by the Signaling Pathways Project website.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000180530 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000048490 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 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. doi:10.1002/j.1460-2075.1995.tb00044.x. PMC   394449 . PMID   7641693.
  6. ↑ 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. S2CID   1042332.
  7. ↑ "Entrez Gene: NRIP1 nuclear receptor interacting protein 1".
  8. ↑ Rosell M, Jones MC, Parker MG (2010). "Role of nuclear receptor corepressor RIP140 in metabolic syndrome". Biochim Biophys Acta. 1812 (8): 919–28. doi:10.1016/j.bbadis.2010.12.016. PMC   3117993 . PMID   21193034.
  9. ↑ 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.
  10. ↑ 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.
  11. ↑ 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 Endocrinol. 21 (11): 2687–97. doi:10.1210/me.2007-0213. PMC   2140279 . PMID   17684114.
  12. ↑ 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.
  13. ↑ 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.
  14. ↑ 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. PMC   1319222 . PMID   16374519.
  15. ↑ 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. Bibcode:2004PNAS..101.8437L. doi: 10.1073/pnas.0401013101 . PMC   420412 . PMID   15155905.
  16. ↑ 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. S2CID   20285964.
  17. ↑ Tullet JM, Pocock V, Steel JH, White R, Milligan S, 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.
  18. ↑ 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.
  19. ↑ "A common denominator of inflammations and fatty liver". News. Science Centric. 2008-05-31. Retrieved 2008-08-31.[ dead link ]
  20. ↑ 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. S2CID   26235707.
  21. ↑ 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.
  22. ↑ 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". Obes Surg. 19 (6): 771–776. doi:10.1007/s11695-009-9834-6. PMID   19367438. S2CID   787869.
  23. ↑ 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. PMC   3112174 . PMID   20410059.
  24. ↑ Zschiedrich I, Hardeland U, Krones-Herzig A, Berriel DM, 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.
  25. ↑ Kumar MB, Tarpey RW, Perdew GH (Aug 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.
  26. 1 2 3 Castet A; 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. 32 (6): 1957–66. doi:10.1093/nar/gkh524. PMC   390375 . PMID   15060175.
  27. ↑ Perissi V; 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. 29 (6): 755–66. doi:10.1016/j.molcel.2008.01.020. PMC   2364611 . PMID   18374649.
  28. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
  29. 1 2 Sugawara T, Abe S, Sakuragi N, Fujimoto Y, Nomura E, Fujieda K, Saito M, Fujimoto S (August 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/endo.142.8.8309 . PMID   11459805.
  30. ↑ Hu X; 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. 279 (1): 319–25. doi: 10.1074/jbc.M307621200 . PMID   14581481.
  31. 1 2 Farooqui M; 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. 42 (4): 971–9. doi:10.1021/bi020497k. PMID   12549917.
  32. 1 2 3 L'Horset F, Dauvois S, Heery DM, Cavaillès V, Parker MG (Nov 1996). "RIP-140 interacts with multiple nuclear receptors by means of two distinct sites". Mol. Cell. Biol. 16 (11): 6029–36. doi:10.1128/MCB.16.11.6029. PMC   231605 . PMID   8887632.
  33. ↑ 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. 272 (18): 12062–8. doi: 10.1074/jbc.272.18.12062 . PMID   9115274.
  34. 1 2 Zilliacus J, Holter E, Wakui H, Tazawa H, Treuter E, Gustafsson JA (Apr 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/mend.15.4.0624 . PMID   11266503.
  35. ↑ Tazawa H; 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. 23 (12): 4187–98. doi:10.1128/MCB.23.12.4187-4198.2003. PMC   156128 . PMID   12773562.
  36. ↑ Subramaniam N, Treuter E, Okret S (Jun 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.
  37. ↑ Mellgren G; 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. 203 (1–2): 91–103. doi:10.1016/S0303-7207(03)00097-2. PMID   12782406. S2CID   733221.

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