Distinct functions for RIP140 in development, inflammation, and metabolism

Trends in Endocrinology and Metabolism

Volumn 24, Issue 9, 2013, Pages 451-459

  Nautiyal, Jaya ^a   Christian, Mark ^b   Parker, Malcolm G ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

Coregulator; Development; Inflammation; Metabolism; Nuclear receptors; RIP140

Indexed keywords

AMPHIREGULIN; ANDROGEN RECEPTOR; AROMATIC HYDROCARBON RECEPTOR; CARNITINE PALMITOYLTRANSFERASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; CYCLIN D1; CYCLIN DEPENDENT KINASE 8; E1A ASSOCIATED P300 PROTEIN; FAT DROPLET; FATTY ACID BINDING PROTEIN; GLUCOCORTICOID RECEPTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HEPATOCYTE NUCLEAR FACTOR 4; HISTONE DEACETYLASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIVER X RECEPTOR; MINERALOCORTICOID RECEPTOR; NUCLEAR RESPIRATORY FACTOR 1; PERILIPIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PREGNANE X RECEPTOR; PROTEIN ARGININE METHYLTRANSFERASE; RECEPTOR INTERACTING PROTEIN 140; RETINOIC ACID BINDING PROTEIN; RETINOIC ACID RECEPTOR; STEROIDOGENIC FACTOR 1; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR E2F; TRANSCRIPTION FACTOR SP1; ZINC FINGER PROTEIN;

ADIPOCYTE; AGING; BREAST DEVELOPMENT; CELL DIFFERENTIATION; CELL PROLIFERATION; CIRCADIAN RHYTHM; COGNITION; CYTOPLASM; FATTY ACID OXIDATION; FATTY ACID TRANSPORT; GENE EXPRESSION; GLUCONEOGENESIS; GLUCOSE TRANSPORT; HEART; HUMAN; INFLAMMATION; LIPOGENESIS; LIVER; MAMMARY GLAND; NONHUMAN; OVULATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; REVIEW; SEXUAL MATURATION;

COREGULATOR; DEVELOPMENT; INFLAMMATION; METABOLISM; NUCLEAR RECEPTORS; RIP140;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ADIPOSE TISSUE; ANIMALS; CHROMATIN ASSEMBLY AND DISASSEMBLY; HUMANS; INFLAMMATION; LIVER; MUSCLE, SKELETAL; MYOCARDIUM; NUCLEAR PROTEINS; RECEPTORS, CYTOPLASMIC AND NUCLEAR;

EID: 84883163079     PISSN: 10432760     EISSN: 18793061     Source Type: Journal    
DOI: 10.1016/j.tem.2013.05.001     Document Type: Review

References (77)

1. Cavailles V., et al. Interaction of proteins with transcriptionally active estrogen receptors. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:10009-10013.
2. Cavailles V., et al. Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor. EMBO J. 1995, 14:3741-3751.
3. Nautiyal J., et al. The transcriptional co-factor RIP140 regulates mammary gland development by promoting the generation of key mitogenic signals. Development 2013, 140:1079-1089.
4. L'Horset F., et al. RIP-140 interacts with multiple nuclear receptors by means of two distinct sites. Mol. Cell. Biol. 1996, 16:6029-6036.
5. White R., et al. The nuclear receptor co-repressor nrip1 (RIP140) is essential for female fertility. Nat. Med. 2000, 6:1368-1374.
6. Leonardsson G., et al. Nuclear receptor corepressor RIP140 regulates fat accumulation. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:8437-8442.
7. Herzog B., et al. 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. 2007, 21:2687-2697.
8. Seth A., et al. The transcriptional corepressor RIP140 regulates oxidative metabolism in skeletal muscle. Cell Metab. 2007, 6:236-245.
9. Fritah A., et al. Elevated expression of the metabolic regulator receptor-interacting protein 140 results in cardiac hypertrophy and impaired cardiac function. Cardiovasc. Res. 2010, 86:443-451.
10. Zschiedrich I., et al. Coactivator function of RIP140 for NFkappaB/RelA-dependent cytokine gene expression. Blood 2008, 112:264-276.
11. Duclot F., et al. Cognitive impairments in adult mice with constitutive inactivation of RIP140 gene expression. Genes Brain Behav. 2012, 11:69-78.
12. Heery D.M., et al. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 1997, 387:733-736.
13. Kiskinis E., et al. RIP140 directs histone and DNA methylation to silence Ucp1 expression in white adipocytes. EMBO J. 2007, 26:4831-4840.
14. Vo N., et al. Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP. Mol. Cell. Biol. 2001, 21:6181-6188.
15. Christian M., et al. Metabolic regulation by the nuclear receptor corepressor RIP140. Trends Endocrinol. Metab. 2006, 17:243-250.
16. Ho P.C., Wei L.N. Biological activities of receptor-interacting protein 140 in adipocytes and metabolic diseases. Curr. Diabetes Rev. 2012, 8:452-457.
17. Mostaqul Huq M.D., et al. Suppression of receptor interacting protein 140 repressive activity by protein arginine methylation. EMBO J. 2006, 25:5094-5104.
18. Mostaqul Huq M.D., et al. Post-translational modifications of nuclear co-repressor RIP140: a therapeutic target for metabolic diseases. Curr. Med. Chem. 2008, 15:386-392.
19. Gupta P., et al. Regulation of co-repressive activity of and HDAC recruitment to RIP140 by site-specific phosphorylation. Mol. Cell. Proteomics 2005, 4:1776-1784.
20. Gupta P., et al. PKCepsilon stimulated arginine methylation of RIP140 for its nuclear-cytoplasmic export in adipocyte differentiation. PLoS ONE 2008, 3:e2658.
21. Rosell M., et al. Role of nuclear receptor corepressor RIP140 in metabolic syndrome. Biochim. Biophys. Acta 2011, 1812:919-928.
22. Fritah A., et al. The metabolic coregulator RIP140: an update. Am. J. Physiol. Endocrinol. Metab. 2010, 299:E335-E340.
23. Christian M., et al. RIP140-targeted repression of gene expression in adipocytes. Mol. Cell. Biol. 2005, 25:9383-9391.
24. Powelka A.M., et al. Suppression of oxidative metabolism and mitochondrial biogenesis by the transcriptional corepressor RIP140 in mouse adipocytes. J. Clin. Invest. 2006, 116:125-136.
25. Hallberg M., et al. A functional interaction between RIP140 and PGC-1alpha regulates the expression of the lipid droplet protein CIDEA. Mol. Cell. Biol. 2008, 28:6785-6795.
26. Docquier A., et al. The transcriptional coregulator RIP140 represses E2F1 activity and discriminates breast cancer subtypes. Clin. Cancer Res. 2010, 16:2959-2970.
27. Docquier A., et al. The RIP140 gene is a transcriptional target of E2F1. PLoS ONE 2012, 7:e35839.
28. Persaud S.D., et al. Gene repressive activity of RIP140 through direct interaction with CDK8. Mol. Endocrinol. 2011, 25:1689-1698.
29. Knuesel M.T., et al. The human CDK8 subcomplex is a molecular switch that controls Mediator coactivator function. Genes Dev. 2009, 23:439-451.
30. Park S.W., et al. RIP140 in thyroid hormone-repression and chromatin remodeling of Crabp1 gene during adipocyte differentiation. Nucleic Acids Res. 2009, 37:7085-7094.
31. Fritah A., et al. Absence of RIP140 reveals a pathway regulating glut4-dependent glucose uptake in oxidative skeletal muscle through UCP1-mediated activation of AMPK. PLoS ONE 2012, 7:e32520.
32. Pedram A., et al. Estrogen inhibits cardiac hypertrophy: role of estrogen receptor-beta to inhibit calcineurin. Endocrinology 2008, 149:3361-3369.
33. Chen Y., et al. Roles of transcriptional corepressor RIP140 and coactivator PGC-1alpha in energy state of chronically infarcted rat hearts and mitochondrial function of cardiomyocytes. Mol. Cell. Endocrinol. 2012, 362:11-18.
34. Berriel Diaz M., et al. Nuclear receptor cofactor receptor interacting protein 140 controls hepatic triglyceride metabolism during wasting in mice. Hepatology 2008, 48:782-791.
35. Green C.B., et al. The meter of metabolism. Cell 2008, 134:728-742.
36. Otway D.T., et al. Rhythmic diurnal gene expression in human adipose tissue from individuals who are lean, overweight, and type 2 diabetic. Diabetes 2011, 60:1577-1581.
37. Poliandri A.H., et al. Modulation of clock gene expression by the transcriptional coregulator receptor interacting protein 140 (RIP140). J. Biol. Rhythms 2011, 26:187-199.
38. Odegaard J.I., Chawla A. Pleiotropic actions of insulin resistance and inflammation in metabolic homeostasis. Science 2013, 339:172-177.
39. Ho P.C., et al. NF-kappaB-mediated degradation of the coactivator RIP140 regulates inflammatory responses and contributes to endotoxin tolerance. Nat. Immunol. 2012, 13:379-386.
40. Coetsier T., Dhont M. Complete and partial luteinized unruptured follicle syndrome after ovarian stimulation with clomiphene citrate/human menopausal gonadotrophin/human chorionic gonadotrophin. Hum. Reprod. 1996, 11:583-587.
41. Tullet J.M., et al. Multiple signaling defects in the absence of RIP140 impair both cumulus expansion and follicle rupture. Endocrinology 2005, 146:4127-4137.
42. Nautiyal J., et al. 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 2010, 151:2923-2932.
43. Edson M.A., et al. The mammalian ovary from genesis to revelation. Endocr. Rev. 2009, 30:624-712.
44. Richards J.S., Pangas S.A. The ovary: basic biology and clinical implications. J. Clin. Invest. 2010, 120:963-972.
45. Ciarloni L., et al. Amphiregulin is an essential mediator of estrogen receptor alpha function in mammary gland development. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:5455-5460.
46. Brisken C., O'Malley B. Hormone action in the mammary gland. Cold Spring Harb. Perspect. Biol. 2010, 2:a003178.
47. McNally S., Martin F. Molecular regulators of pubertal mammary gland development. Ann. Med. 2011, 43:212-234.
48. Mallepell S., et al. Paracrine signaling through the epithelial estrogen receptor alpha is required for proliferation and morphogenesis in the mammary gland. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:2196-2201.
49. Van Keymeulen A., et al. Distinct stem cells contribute to mammary gland development and maintenance. Nature 2011, 479:189-193.
50. Stingl J., et al. Purification and unique properties of mammary epithelial stem cells. Nature 2006, 439:993-997.
51. Lee S., et al. Alterations of gene expression in the development of early hyperplastic precursors of breast cancer. Am. J. Pathol. 2007, 171:252-262.
52. Hannafon B.N., et al. Expression of microRNA and their gene targets are dysregulated in preinvasive breast cancer. Breast Cancer Res. 2011, 13:R24.
53. Oh D.S., et al. Estrogen-regulated genes predict survival in hormone receptor-positive breast cancers. J. Clin. Oncol. 2006, 24:1656-1664.
54. Chan C.M., et al. Expression of nuclear receptor interacting proteins TIF-1, SUG-1, receptor interacting protein 140, and corepressor SMRT in tamoxifen-resistant breast cancer. Clin. Cancer Res. 1999, 5:3460-3467.
55. Han S.J., et al. Steroid receptor coactivator (SRC)-1 and SRC-3 differentially modulate tissue-specific activation functions of the progesterone receptor. Mol. Endocrinol. 2006, 20:45-55.
56. Howlin J., et al. CITED1 homozygous null mice display aberrant pubertal mammary ductal morphogenesis. Oncogene 2006, 25:1532-1542.
57. Jiang P., et al. Key roles for MED1 LxxLL motifs in pubertal mammary gland development and luminal-cell differentiation. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:6765-6770.
58. Zwart W., et al. Oestrogen receptor-co-factor-chromatin specificity in the transcriptional regulation of breast cancer. EMBO J. 2011, 30:4764-4776.
59. Fenner M.H., Elstner E. Peroxisome proliferator-activated receptor-gamma ligands for the treatment of breast cancer. Expert Opin. Investig. Drugs 2005, 14:557-568.
60. Riggins R.B., et al. Orphan nuclear receptors in breast cancer pathogenesis and therapeutic response. Endocr. Relat. Cancer 2010, 17:R213-R231.
61. Giordano C., et al. Farnesoid X receptor inhibits tamoxifen-resistant MCF-7 breast cancer cell growth through downregulation of HER2 expression. Oncogene 2011, 30:4129-4140.
62. Hou J.C., Pessin J.E. Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking. Curr. Opin. Cell Biol. 2007, 19:466-473.
63. Sakamoto K., Holman G.D. Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic. Am. J. Physiol. Endocrinol. Metab. 2008, 295:E29-E37.
64. Ho P.C., et al. A negative regulatory pathway of GLUT4 trafficking in adipocyte: new function of RIP140 in the cytoplasm via AS160. Cell Metab. 2009, 10:516-523.
65. Ho P.C., et al. Cytoplasmic receptor-interacting protein 140 (RIP140) interacts with perilipin to regulate lipolysis. Cell. Signal. 2011, 23:1396-1403.
66. Ho P.C., Wei L.N. Negative regulation of adiponectin secretion by receptor interacting protein 140 (RIP140). Cell. Signal. 2012, 24:71-76.
67. Gardiner K., et al. Down syndrome: from understanding the neurobiology to therapy. J. Neurosci. 2010, 30:14943-14945.
68. Tsai N.P., et al. MicroRNA mir-346 targets the 5'-untranslated region of receptor-interacting protein 140 (RIP140) mRNA and up-regulates its protein expression. Biochem. J. 2009, 424:411-418.
69. Zhu Y., et al. A MicroRNA gene is hosted in an intron of a schizophrenia-susceptibility gene. Schizophr. Res. 2009, 109:86-89.
70. Yuan R., et al. Genetic coregulation of age of female sexual maturation and lifespan through circulating IGF1 among inbred mouse strains. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:8224-8229.
71. Hellal-Levy C., et al. Crucial role of the H11-H12 loop in stabilizing the active conformation of the human mineralocorticoid receptor. Mol. Endocrinol. 2000, 14:1210-1221.
72. Zilliacus J., et al. Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140. Mol. Endocrinol. 2001, 15:501-511.
73. Castet A., et al. Multiple domains of the Receptor-Interacting Protein 140 contribute to transcription inhibition. Nucleic Acids Res. 2004, 32:1957-1966.
74. Kumar M.B., et al. Differential recruitment of coactivator RIP140 by Ah and estrogen receptors. Absence of a role for LXXLL motifs. J. Biol. Chem. 1999, 274:22155-22164.
75. Lopez-Garcia J., et al. ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylases. Nucleic Acids Res. 2006, 34:6126-6136.
76. Teyssier C., et al. Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-induced activator protein-1 activity by reversing glucocorticoid receptor-interacting protein 1 effect. Mol. Endocrinol. 2003, 17:287-299.
77. Wei L.N., et al. Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing. J. Biol. Chem. 2000, 275:40782-40787.