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PPAR Research
Volume 2007, Article ID 53843, 11 pages
http://dx.doi.org/10.1155/2007/53843
Review Article

Nuclear Receptor Cofactors in PPARγ-Mediated Adipogenesis and Adipocyte Energy Metabolism

McArdle Laboratory for Cancer Research, University of Wisconsin, 1400 University Avenue, Madison, WI 53706, USA

Received 14 July 2006; Revised 17 October 2006; Accepted 17 October 2006

Academic Editor: Francine M. Gregoire

Copyright © 2007 Emily Powell et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. I. Issemann and S. Green, “Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators,” Nature, vol. 347, no. 6294, pp. 645–650, 1990. View at Publisher · View at Google Scholar
  2. J. Berger and D. E. Moller, “The mechanisms of action of PPARs,” Annual Review of Medicine, vol. 53, no. 1, pp. 409–435, 2002. View at Publisher · View at Google Scholar
  3. R. M. Evans, G. D. Barish, and Y.-X. Wang, “PPARs and the complex journey to obesity,” Nature Medicine, vol. 10, no. 4, pp. 355–361, 2004. View at Publisher · View at Google Scholar
  4. J. N. Feige, L. Gelman, L. Michalik, B. Desvergne, and W. Wahli, “From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions,” Progress in Lipid Research, vol. 45, no. 2, pp. 120–159, 2006. View at Publisher · View at Google Scholar
  5. A. J. Vidal-Puig, R. V. Considine, M. Jimenez-Liñan et al., “Peroxisome proliferator-activated receptor gene expression in human tissues: effects of obesity, weight loss, and regulation by insulin and glucocorticoids,” Journal of Clinical Investigation, vol. 99, no. 10, pp. 2416–2422, 1997. View at Google Scholar
  6. D. Ren, T. N. Collingwood, E. J. Rebar, A. P. Wolffe, and H. S. Camp, “PPARγ knockdown by engineered transcription factors: exogenous PPARγ2 but not PPARγ1 reactivates adipogenesis,” Genes & Development, vol. 16, no. 1, pp. 27–32, 2002. View at Publisher · View at Google Scholar
  7. A. Werman, A. Hollenberg, G. Solanes, C. Bjørbæk, A. J. Vidal-Puig, and J. S. Flier, “Ligand-independent activation domain in the N terminus of peroxisome proliferator-activated receptor γ (PPARγ). Differential activity of PPARγ1 and -2 isoforms and influence of insulin,” Journal of Biological Chemistry, vol. 272, no. 32, pp. 20230–20235, 1997. View at Publisher · View at Google Scholar
  8. P. Tontonoz, E. Hu, and B. M. Spiegelman, “Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid-activated transcription factor,” Cell, vol. 79, no. 7, pp. 1147–1156, 1994. View at Publisher · View at Google Scholar
  9. P. Tontonoz, E. Hu, R. A. Graves, A. I. Budavari, and B. M. Spiegelman, “mPPARγ2: tissue-specific regulator of an adipocyte enhancer,” Genes & Development, vol. 8, no. 10, pp. 1224–1234, 1994. View at Google Scholar
  10. S. Yu, N. Viswakarma, S. K. Batra, M. Sambasiva Rao, and J. K. Reddy, “Identification of promethin and PGLP as two novel up-regulated genes in PPARγ1-induced adipogenic mouse liver,” Biochimie, vol. 86, no. 11, pp. 743–761, 2004. View at Publisher · View at Google Scholar
  11. A. Chawla, E. J. Schwarz, D. D. Dimaculangan, and M. A. Lazar, “Peroxisome proliferator-activated receptor (PPAR) γ: adipose-predominant expression and induction early in adipocyte differentiation,” Endocrinology, vol. 135, no. 2, pp. 798–800, 1994. View at Publisher · View at Google Scholar
  12. L. Gelman, J.-C. Fruchart, and J. Auwerx, “An update on the mechanisms of action of the peroxisome proliferator-activated receptors (PPARs) and their roles in inflammation and cancer,” Cellular and Molecular Life Sciences, vol. 55, no. 6-7, pp. 932–943, 1999. View at Publisher · View at Google Scholar
  13. M. Lehrke and M. A. Lazar, “The many faces of PPARγ,” Cell, vol. 123, no. 6, pp. 993–999, 2005. View at Publisher · View at Google Scholar
  14. J. Torchia, C. Glass, and M. G. Rosenfeld, “Co-activators and co-repressors in the integration of transcriptional responses,” Current Opinion in Cell Biology, vol. 10, no. 3, pp. 373–383, 1998. View at Publisher · View at Google Scholar
  15. S. A. Kliewer, K. Umesono, D. J. Noonan, R. A. Heyman, and R. M. Evans, “Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors,” Nature, vol. 358, no. 6389, pp. 771–774, 1992. View at Publisher · View at Google Scholar
  16. M. G. Rosenfeld, V. V. Lunyak, and C. K. Glass, “Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response,” Genes & Development, vol. 20, no. 11, pp. 1405–1428, 2006. View at Publisher · View at Google Scholar
  17. O. Hermanson, C. K. Glass, and M. G. Rosenfeld, “Nuclear receptor coregulators: multiple modes of modification,” Trends in Endocrinology and Metabolism, vol. 13, no. 2, pp. 55–60, 2002. View at Publisher · View at Google Scholar
  18. S. Westin, M. G. Rosenfeld, and C. K. Glass, “Nuclear receptor coactivators,” Advances in Pharmacology, vol. 47, pp. 89–112, 2000. View at Google Scholar
  19. L. Xu, C. K. Glass, and M. G. Rosenfeld, “Coactivator and corepressor complexes in nuclear receptor function,” Current Opinion in Genetics & Development, vol. 9, no. 2, pp. 140–147, 1999. View at Publisher · View at Google Scholar
  20. D. M. Heery, S. Hoare, S. Hussain, M. G. Parker, and H. Sheppard, “Core LXXLL motif sequences in CREB-binding protein, SRC1, and RIP140 define affinity and selectivity for steroid and retinoid receptors,” Journal of Biological Chemistry, vol. 276, no. 9, pp. 6695–6702, 2001. View at Publisher · View at Google Scholar
  21. D. M. Heery, E. Kalkhoven, S. Hoare, and M. G. Parker, “A signature motif in transcriptional co-activators mediates binding to nuclear receptors,” Nature, vol. 387, no. 6634, pp. 733–736, 1997. View at Publisher · View at Google Scholar
  22. C. Leo and J. D. Chen, “The SRC family of nuclear receptor coactivators,” Gene, vol. 245, no. 1, pp. 1–11, 2000. View at Publisher · View at Google Scholar
  23. W. Xu, “Nuclear receptor coactivators: the key to unlock chromatin,” Biochemistry and Cell Biology, vol. 83, no. 4, pp. 418–428, 2005. View at Publisher · View at Google Scholar
  24. J. A. Martens and F. Winston, “Recent advances in understanding chromatin remodeling by Swi/Snf complexes,” Current Opinion in Genetics & Development, vol. 13, no. 2, pp. 136–142, 2003. View at Publisher · View at Google Scholar
  25. N. Salma, H. Xiao, E. Mueller, and A. N. Imbalzano, “Temporal recruitment of transcription factors and SWI/SNF chromatin-remodeling enzymes during adipogenic induction of the peroxisome proliferator-activated receptor γ nuclear hormone receptor,” Molecular and Cellular Biology, vol. 24, no. 11, pp. 4651–4663, 2004. View at Publisher · View at Google Scholar
  26. M. B. Debril, L. Gelman, E. Fayard, J. S. Annicotte, S. Rocchi, and J. Auwerx, “Transcription factors and nuclear receptors interact with the SWI/SNF complex through the BAF60c subunit,” Journal of Biological Chemistry, vol. 279, no. 16, pp. 16677–16686, 2004. View at Publisher · View at Google Scholar
  27. J. D. Fondell, H. Ge, and R. G. Roeder, “Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 16, pp. 8329–8333, 1996. View at Publisher · View at Google Scholar
  28. C. Rachez, B. D. Lemon, Z. Suldan et al., “Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex,” Nature, vol. 398, no. 6730, pp. 824–828, 1999. View at Publisher · View at Google Scholar
  29. R. G. Roeder, “Role of general and gene-specific cofactors in the regulation of eukaryotic transcription,” Cold Spring Harbor Symposia on Quantitative Biology, vol. 63, pp. 201–218, 1998. View at Publisher · View at Google Scholar
  30. S. Malik and R. G. Roeder, “Transcriptional regulation through Mediator-like coactivators in yeast and metazoan cells,” Trends in Biochemical Sciences, vol. 25, no. 6, pp. 277–283, 2000. View at Publisher · View at Google Scholar
  31. K. Ge, M. Guermah, C. X. Yuan et al., “Transcription coactivator TRAP220 is required for PPAR ? 2-stimulated adipogenesis,” Nature, vol. 417, no. 6888, pp. 563–567, 2002. View at Publisher · View at Google Scholar
  32. P. Puigserver, G. Adelmant, Z. Wu et al., “Activation of PPAR? coactivator-1 through transcription factor docking,” Science, vol. 286, no. 5443, pp. 1368–1371, 1999. View at Publisher · View at Google Scholar
  33. A. E. Wallberg, S. Yamamura, S. Malik, B. M. Spiegelman, and R. G. Roeder, “Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1α,” Molecular Cell, vol. 12, no. 5, pp. 1137–1149, 2003. View at Publisher · View at Google Scholar
  34. M. Monsalve, Z. Wu, G. Adelmant, P. Puigserver, M. Fan, and B. M. Spiegelman, “Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1,” Molecular Cell, vol. 6, no. 2, pp. 307–316, 2000. View at Publisher · View at Google Scholar
  35. P. Puigserver and B. M. Spiegelman, “Peroxisome proliferator-activated receptor-γ coactivator 1 α (PGC-1 α): transcriptional coactivator and metabolic regulator,” Endocrine Reviews, vol. 24, no. 1, pp. 78–90, 2003. View at Publisher · View at Google Scholar
  36. J. Lin, C. Handschin, and B. M. Spiegelman, “Metabolic control through the PGC-1 family of transcription coactivators,” Cell Metabolism, vol. 1, no. 6, pp. 361–370, 2005. View at Publisher · View at Google Scholar
  37. A. J. Horlein, A. M. Naar, T. Heinzel et al., “Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor,” Nature, vol. 377, no. 6548, pp. 397–404, 1995. View at Publisher · View at Google Scholar
  38. J. D. Chen and R. M. Evans, “A transcriptional co-repressor that interacts with nuclear hormone receptors,” Nature, vol. 377, no. 6548, pp. 454–457, 1995. View at Publisher · View at Google Scholar
  39. P. Dowell, J. E. Ishmael, D. Avram, V. J. Peterson, D. J. Nevrivy, and M. Leid, “Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor α interacting protein,” Journal of Biological Chemistry, vol. 274, no. 22, pp. 15901–15907, 1999. View at Publisher · View at Google Scholar
  40. T. B. Stanley, L. M. Leesnitzer, V. G. Montana et al., “Subtype specific effects of peroxisome proliferator-activated receptor ligands on corepressor affinity,” Biochemistry, vol. 42, no. 31, pp. 9278–9287, 2003. View at Publisher · View at Google Scholar
  41. A-M. Krogsdam, C. A. Nielsen, S. Neve et al., “Nuclear receptor corepressor-dependent repression of peroxisome-proliferator-activated receptor d-mediated transactivation,” Biochemical Journal, vol. 363, no. pt 1, pp. 157–165, 2002. View at Publisher · View at Google Scholar
  42. C. Yu, K. Markan, K. A. Temple, D. Deplewski, M. J. Brady, and R. N. Cohen, “The nuclear receptor corepressors NCoR and SMRT decrease peroxisome proliferator-activated receptor γ transcriptional activity and repress 3T3-L1 adipogenesis,” Journal of Biological Chemistry, vol. 280, no. 14, pp. 13600–13605, 2005. View at Publisher · View at Google Scholar
  43. F. Picard, M. Kurtev, N. Chung et al., “Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-?,” Nature, vol. 429, no. 6993, pp. 771–776, 2004. View at Publisher · View at Google Scholar
  44. V. Perissi and M. G. Rosenfeld, “Controlling nuclear receptors: the circular logic of cofactor cycles,” Nature Reviews. Molecular Cell Biology, vol. 6, no. 7, pp. 542–554, 2005. View at Publisher · View at Google Scholar
  45. H. G. Yoon, D. W. Chan, Z. Q. Huang et al., “Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1,” EMBO Journal, vol. 22, no. 6, pp. 1336–1346, 2003. View at Publisher · View at Google Scholar
  46. V. Perissi, A. Aggarwal, C. K. Glass, D. W. Rose, and M. G. Rosenfeld, “A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors,” Cell, vol. 116, no. 4, pp. 511–526, 2004. View at Publisher · View at Google Scholar
  47. M. L. Privalsky, “The role of corepressors in transcriptional regulation by nuclear hormone receptors,” Annual Review of Physiology, vol. 66, pp. 315–360, 2004. View at Publisher · View at Google Scholar
  48. N. J. McKenna and B. W. O'Malley, “From ligand to response: generating diversity in nuclear receptor coregulator function,” Journal of Steroid Biochemistry and Molecular Biology, vol. 74, no. 5, pp. 351–356, 2000. View at Publisher · View at Google Scholar
  49. J. Xu and B. W. O'Malley, “Molecular mechanisms and cellular biology of the steroid receptor coactivator (SRC) family in steroid receptor function,” Reviews in Endocrine & Metabolic Disorders, vol. 3, no. 3, pp. 185–192, 2002. View at Publisher · View at Google Scholar
  50. F. Picard, M. Gehin, J. Annicotte et al., “SRC-1 and TIF2 control energy balance between white and brown adipose tissues,” Cell, vol. 111, no. 7, pp. 931–941, 2002. View at Publisher · View at Google Scholar
  51. Z. Wang, C. Qi, A. Krones et al., “Critical roles of the p160 transcriptional coactivators p/CIP and SRC-1 in energy balance,” Cell Metabolism, vol. 3, no. 2, pp. 111–122, 2006. View at Publisher · View at Google Scholar
  52. M. Uldry, W. Yang, J. St-Pierre, J. Lin, P. Seale, and B. M. Spiegelman, “Complementary action of the PGC-1 coactivators in mitochondrial biogenesis and brown fat differentiation,” Cell Metabolism, vol. 3, no. 5, pp. 333–341, 2006. View at Publisher · View at Google Scholar
  53. J. Lin, P. H. Wu, P. T. Tarr et al., “Defects in adaptive energy metabolism with CNS-linked hyperactivity in PGC-1a null mice,” Cell, vol. 119, no. 1, pp. 121–135, 2004. View at Publisher · View at Google Scholar
  54. Y. Barak, M. C. Nelson, E. S. Ong et al., “PPAR ? is required for placental, cardiac, and adipose tissue development,” Molecular Cell, vol. 4, no. 4, pp. 585–595, 1999. View at Publisher · View at Google Scholar
  55. Y. Zhu, L. Kan, C. Qi et al., “Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR,” Journal of Biological Chemistry, vol. 275, no. 18, pp. 13510–13516, 2000. View at Publisher · View at Google Scholar
  56. P. Antonson, G. U. Schuster, L. Wang et al., “Inactivation of the nuclear receptor coactivator RAP250 in mice results in placental vascular dysfunction,” Molecular and Cellular Biology, vol. 23, no. 4, pp. 1260–1268, 2003. View at Publisher · View at Google Scholar
  57. Y. J. Zhu, S. E. Crawford, V. Stellmach et al., “Coactivator PRIP, the peroxisome proliferator-activated receptor-interacting protein, is a modulator of placental, cardiac, hepatic, and embryonic development,” Journal of Biological Chemistry, vol. 278, no. 3, pp. 1986–1990, 2003. View at Publisher · View at Google Scholar
  58. G. Leonardsson, J. H. Steel, M. Christian et al., “Nuclear receptor corepressor RIP140 regulates fat accumulation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 22, pp. 8437–8442, 2004. View at Publisher · View at Google Scholar
  59. P. Puigserver, Z. Wu, C. W. Park, R. Graves, M. Wright, and B. M. Spiegelman, “A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis,” Cell, vol. 92, no. 6, pp. 829–839, 1998. View at Publisher · View at Google Scholar
  60. Y. Wu, W. W. Chin, Y. Wang, and T. P. Burris, “Ligand and coactivator identity determines the requirement of the charge clamp for coactivation of the peroxisome proliferator-activated receptor γ,” Journal of Biological Chemistry, vol. 278, no. 10, pp. 8637–8644, 2003. View at Publisher · View at Google Scholar
  61. H. P. Guan, T. Ishizuka, P. C. Chui, M. Lehrke, and M. A. Lazar, “Corepressors selectively control the transcriptional activity of PPARγ in adipocytes,” Genes & Development, vol. 19, no. 4, pp. 453–461, 2005. View at Publisher · View at Google Scholar
  62. Z. Wu, P. Puigserver, and U. Andersson, “Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1,” Cell, vol. 98, no. 1, pp. 115–124, 1999. View at Publisher · View at Google Scholar
  63. C. Tiraby and D. Langin, “Conversion from white to brown adipocytes: a strategy for the control of fat mass?” Trends in Endocrinology and Metabolism, vol. 14, no. 10, pp. 439–441, 2003. View at Publisher · View at Google Scholar
  64. K. Tsukiyama-Kohara, F. Poulin, M. Kohara et al., “Adipose tissue reduction in mice lacking the translational inhibitor 4E-BP1,” Nature Medicine, vol. 7, no. 10, pp. 1128–1132, 2001. View at Publisher · View at Google Scholar
  65. A. Cederberg, L. M. Gronning, B. Ahren, K. Tasken, P. Carlsson, and S. Enerback, “FOXC2 is a winged helix gene that counteracts obesity, hypertriglyceridemia, and diet-induced insulin resistance,” Cell, vol. 106, no. 5, pp. 563–573, 2001. View at Publisher · View at Google Scholar
  66. J. Kopecky, G. Clarke, S. Enerback, B. Spiegelman, and L. P. Kozak, “Expression of the mitochondrial uncoupling protein gene from the aP2 gene promoter prevents genetic obesity,” Journal of Clinical Investigation, vol. 96, no. 6, pp. 2914–2923, 1995. View at Google Scholar
  67. J. Lin, P. Puigserver, J. Donovan, P. Tarr, and B. M. Spiegelman, “Peroxisome proliferator-activated receptor γ coactivator 1β (PGC-1β ), a novel PGC-1-related transcription coactivator associated with host cell factor,” Journal of Biological Chemistry, vol. 277, no. 3, pp. 1645–1648, 2002. View at Publisher · View at Google Scholar
  68. J. Lin, P. T. Tarr, R. Yang et al., “PGC-1ß in the regulation of hepatic glucose and energy metabolism,” Journal of Biological Chemistry, vol. 278, no. 33, pp. 30843–30848, 2003. View at Publisher · View at Google Scholar
  69. J. St-Pierre, J. Lin, S. Krauss et al., “Bioenergetic analysis of peroxisome proliferator-activated receptor ? coactivators 1a and 1ß (PGC-1a and PGC-1ß) in muscle cells,” Journal of Biological Chemistry, vol. 278, no. 29, pp. 26597–26603, 2003. View at Publisher · View at Google Scholar
  70. L. Gelman, G. Zhou, L. Fajas, E. Raspe, J. C. Fruchart, and J. Auwerx, “p300 interacts with the N- and C-terminal part of PPARγ2 in a ligand-independent and -dependent manner, respectively,” Journal of Biological Chemistry, vol. 274, no. 12, pp. 7681–7688, 1999. View at Publisher · View at Google Scholar
  71. N. Takahashi, T. Kawada, T. Yamamoto et al., “Overexpression and ribozyme-mediated targeting of transcriptional coactivators CREB-binding protein and p300 revealed their indispensable roles in adipocyte differentiation through the regulation of peroxisome proliferator-activated receptor ?,” Journal of Biological Chemistry, vol. 277, no. 19, pp. 16906–16912, 2002. View at Publisher · View at Google Scholar
  72. S. Sif, A. J. Saurin, A. N. Imbalzano, and R. E. Kingston, “Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes,” Genes & Development, vol. 15, no. 5, pp. 603–618, 2001. View at Publisher · View at Google Scholar
  73. S. Bultman, T. Gebuhr, D. Yee et al., “A Brg1 null mutation in the mouse reveals functional differences among mammalian SWI/SNF complexes,” Molecular Cell, vol. 6, no. 6, pp. 1287–1295, 2000. View at Publisher · View at Google Scholar
  74. J. C. Reyes, J. Barra, C. Muchardt, A. Camus, C. Babinet, and M. Yaniv, “Altered control of cellular proliferation in the absence of mammalian brahma (SNF2α),” EMBO Journal, vol. 17, no. 23, pp. 6979–6991, 1998. View at Publisher · View at Google Scholar
  75. B. Lemon, C. Inouye, D. S. King, and R. Tjian, “Selectivity of chromatin-remodelling cofactors for ligand-activated transcription,” Nature, vol. 414, no. 6866, pp. 924–928, 2001. View at Publisher · View at Google Scholar
  76. C. X. Yuan, M. Ito, J. D. Fondell, Z. Y. Fu, and R. G. Roeder, “The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 14, pp. 7939–7944, 1998. View at Publisher · View at Google Scholar
  77. Y. Zhu, C. Qi, S. Jain, M. S. Rao, and J. K. Reddy, “Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor,” Journal of Biological Chemistry, vol. 272, no. 41, pp. 25500–25506, 1997. View at Publisher · View at Google Scholar
  78. Y. Zhu, C. Qi, Y. Jia, J. S. Nye, M. S. Rao, and J. K. Reddy, “Deletion of PBP/PPARBP, the gene for nuclear receptor coactivator peroxisome proliferator-activated receptor-binding protein, results in embryonic lethality,” Journal of Biological Chemistry, vol. 275, no. 20, pp. 14779–14782, 2000. View at Publisher · View at Google Scholar
  79. F. Caira, P. Antonson, M. Pelto-Huikko, E. Treuter, and J. A. Gustafsson, “Cloning and characterization of RAP250, a novel nuclear receptor coactivator,” Journal of Biological Chemistry, vol. 275, no. 8, pp. 5308–5317, 2000. View at Publisher · View at Google Scholar
  80. Y . Zhu, C. Qi, W.-Q. Cao et al., “Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 18, pp. 10380–10385, 2001. View at Publisher · View at Google Scholar
  81. P. Misra, C. Qi, S. Yu et al., “Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation,” Journal of Biological Chemistry, vol. 277, no. 22, pp. 20011–20019, 2002. View at Publisher · View at Google Scholar
  82. S. Surapureddi, S. Yu, H. Bu et al., “Identification of a transcriptionally active peroxisome proliferator-activated receptor a -interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 18, pp. 11836–11841, 2002. View at Publisher · View at Google Scholar
  83. V. Cavailles, S. Dauvois, F. L'Horset et al., “Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor,” EMBO Journal, vol. 14, no. 15, pp. 3741–3751, 1995. View at Google Scholar
  84. E. Treuter, T. Albrektsen, L. Johansson, J. Leers, and J. A. Gustafsson, “A regulatory role for RIP140 in nuclear receptor activation,” Molecular Endocrinology, vol. 12, no. 6, pp. 864–881, 1998. View at Publisher · View at Google Scholar
  85. X. Hu and M. A. Lazar, “The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors,” Nature, vol. 402, no. 6757, pp. 93–96, 1999. View at Publisher · View at Google Scholar
  86. L. Nagy, H. Y. Kao, J. D. Love et al., “Mechanism of corepressor binding and release from nuclear hormone receptors,” Genes & Development, vol. 13, no. 24, pp. 3209–3216, 1999. View at Publisher · View at Google Scholar
  87. V. Perissi, L. M. Staszewski, E. M. McInerney et al., “Molecular determinants of nuclear receptor-corepressor interaction,” Genes & Development, vol. 13, no. 24, pp. 3198–3208, 1999. View at Publisher · View at Google Scholar
  88. A.-M. Krogsdam, C. A. Nielsen, S. Neve et al., “Nuclear receptor corepressor-dependent repression of peroxisome-proliferator-activated receptor d-mediated transactivation,” Biochemical Journal, vol. 363, no. pt 1, pp. 157–165, 2002. View at Publisher · View at Google Scholar
  89. H. P. Guan, T. Ishizuka, P. C. Chui, M. Lehrke, and M. A. Lazar, “Corepressors selectively control the transcriptional activity of PPARγ in adipocytes,” Genes & Development, vol. 19, no. 4, pp. 453–461, 2005. View at Publisher · View at Google Scholar
  90. F. Picard, M. Kurtev, N. Chung et al., “Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-?,” Nature, vol. 429, no. 6993, pp. 771–776, 2004. View at Publisher · View at Google Scholar
  91. Y. Kodera, K. Takeyama, A. Murayama, M. Suzawa, Y. Masuhiro, and S. Kato, “Ligand type-specific interactions of peroxisome proliferator-activated receptor γ with transcriptional coactivators,” Journal of Biological Chemistry, vol. 275, no. 43, pp. 33201–33204, 2000. View at Publisher · View at Google Scholar