Tissue- and Nuclear Receptor-Specific Function of the C-Terminal LXXLL Motif of Coactivator NCoA6/AIB3 in Mice

REFERENCES

• Albers, M., B. Blume, T. Schlueter, M. B. Wright, I. Kober, C. Kremoser, U. Deuschle, and M. Koegl. 2006. A novel principle for partial agonism of liver X receptor ligands. Competitive recruitment of activators and repressors. J. Biol. Chem. 281:4920–4930.
   PubMedGoogle Scholar
• Alberti, S., G. Schuster, P. Parini, D. Feltkamp, U. Diczfalusy, M. Rudling, B. Angelin, I. Bjorkhem, S. Pettersson, and J. A. Gustafsson. 2001. Hepatic cholesterol metabolism and resistance to dietary cholesterol in LXRβ-deficient mice. J. Clin. Investig. 107:565–573.
   PubMed Web of Science ®Google Scholar
• Antonson, P. G., U. Schuster, L. Wang, B. Rozell, E. Holter, P. Flodby, E. Treuter, L. Holmgren, and J. A. Gustafsson. 2003. Inactivation of the nuclear receptor coactivator RAP250 in mice results in placental vascular dysfunction. Mol. Cell. Biol. 23:1260–1268.
   PubMed Web of Science ®Google Scholar
• Caira, F., P. Antonson, M. Pelto-Huikko, E. Treuter, and J. A. Gustafsson. 2000. Cloning and characterization of RAP250, a novel nuclear receptor coactivator. J. Biol. Chem. 275:5308–5317.
   PubMed Web of Science ®Google Scholar
• Chiang, J. Y. 2002. Bile acid regulation of gene expression: roles of nuclear hormone receptors. Endocr. Rev. 23:443–463.
   PubMed Web of Science ®Google Scholar
• Couse, J. F., and K. S. Korach. 1999. Estrogen receptor null mice: what have we learned and where will they lead us? Endocr Rev. 20:358–417.
   PubMed Web of Science ®Google Scholar
• Goo, Y. H., Y. C. Sohn, D. H. Kim, S. W. Kim, M. J. Kang, D. J. Jung, E. Kwak, N. A. Barlev, S. L. Berger, V. T. Chow, R. G. Roeder, D. O. Azorsa, P. S. Meltzer, P. G. Suh, E. J. Song, K. J. Lee, Y. C. Lee, and J. W. Lee. 2003. Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. Mol. Cell. Biol. 23:140–149.
   PubMed Web of Science ®Google Scholar
• Grefhorst, A., B. M. Elzinga, P. J. Voshol, T. Plosch, T. Kok, V. W. Bloks, F. H. van der Sluijs, L. M. Havekes, J. A. Romijn, H. J. Verkade, and F. Kuipers. 2002. Stimulation of lipogenesis by pharmacological activation of the liver X receptor leads to production of large, triglyceride-rich very low density lipoprotein particles. J. Biol. Chem. 277:34182–34190.
   PubMed Web of Science ®Google Scholar
• Guan, X. Y., J. Xu, S. L. Anzick, H. Zhang, J. M. Trent, and P. S. Meltzer. 1996. Hybrid selection of transcribed sequences from microdissected DNA: isolation of genes within amplified region at 20q11-q13.2 in breast cancer. Cancer Res. 56:3446–3450.
   PubMedGoogle Scholar
• Heery, D. M., E. Kalkhoven, S. Hoare, and M. G. Parker. 1997. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733–736.
   PubMed Web of Science ®Google Scholar
• Iwasaki, T., W. W. Chin, and L. Ko. 2001. Identification and characterization of RRM-containing coactivator activator (CoAA) as TRBP-interacting protein, and its splice variant as a coactivator modulator (CoAM). J. Biol. Chem. 276:33375–33383.
   PubMedGoogle Scholar
• Jolley, C. D., J. M. Dietschy, and S. D. Turley. 1999. Genetic differences in cholesterol absorption in 129/Sv and C57BL/6 mice: effect on cholesterol responsiveness. Am. J. Physiol. 276:G1117–G1124.
   PubMedGoogle Scholar
• Joseph, S. B., B. A. Laffitte, P. H. Patel, M. A. Watson, K. E. Matsukuma, R. Walczak, J. L. Collins, T. F. Osborne, and P. Tontonoz. 2002. Direct and indirect mechanisms for regulation of fatty acid synthase gene expression by liver X receptors. J. Biol. Chem. 277:11019–11025.
   PubMed Web of Science ®Google Scholar
• Kim, S. W., C. Cheong, Y. C. Sohn, Y. H. Goo, W. J. Oh, J. H. Park, S. Y. Joe, H. S. Kang, D. K. Kim, C. Kee, J. W. Lee, and H. W. Lee. 2002. Multiple developmental defects derived from impaired recruitment of ASC-2 to nuclear receptors in mice: implication for posterior lenticonus with cataract. Mol. Cell. Biol. 22:8409–8414.
   PubMedGoogle Scholar
• Kim, S. W., K. Park, E. Kwak, E. Choi, S. Lee, J. Ham, H. Kang, J. M. Kim, S. Y. Hwang, Y. Y. Kong, K. Lee, and J. W. Lee. 2003. Activating signal cointegrator 2 required for liver lipid metabolism mediated by liver X receptors in mice. Mol. Cell. Biol. 23:3583–3592.
   PubMedGoogle Scholar
• Ko, L., G. R. Cardona, and W. W. Chin. 2000. Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator. Proc. Natl. Acad. Sci. USA 97:6212–6217.
   PubMedGoogle Scholar
• Korach, K. S., J. F. Couse, S. W. Curtis, T. F. Washburn, J. Lindzey, K. S. Kimbro, E. M. Eddy, S. Migliaccio, S. M. Snedeker, D. B. Lubahn, D. W. Schomberg, and E. P. Smith. 1996. Estrogen receptor gene disruption: molecular characterization and experimental and clinical phenotypes. Recent Prog. Horm. Res. 51:159–186.
   PubMedGoogle Scholar
• Kuang, S. Q., L. Liao, H. Zhang, F. A. Pereira, Y. Yuan, F. J. DeMayo, L. Ko, and J. Xu. 2002. Deletion of the cancer-amplified coactivator AIB3 results in defective placentation and embryonic lethality. J. Biol. Chem. 277:45356–45360.
   PubMed Web of Science ®Google Scholar
• Lee, S., D. K. Lee, Y. Dou, J. Lee, B. Lee, E. Kwak, Y. Y. Kong, S. K. Lee, R. G. Roeder, and J. W. Lee. 2006. Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases. Proc. Natl. Acad. Sci. USA 103:15392–15397.
   PubMed Web of Science ®Google Scholar
• Lee, S. K., S. L. Anzick, J. E. Choi, L. Bubendorf, X. Y. Guan, Y. K. Jung, O. P. Kallioniemi, J. Kononen, J. M. Trent, D. Azorsa, B. H. Jhun, J. H. Cheong, Y. C. Lee, P. S. Meltzer, and J. W. Lee. 1999. A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J. Biol. Chem. 274:34283–34293.
   PubMed Web of Science ®Google Scholar
• Lee, S. K., S. Y. Jung, Y. S. Kim, S. Y. Na, Y. C. Lee, and J. W. Lee. 2001. Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2. Mol. Endocrinol. 15:241–254.
   PubMedGoogle Scholar
• Levy, E., S. Spahis, D. Sinnett, N. Peretti, F. Maupas-Schwalm, E. Delvin, M. Lambert, and M. A. Lavoie. 2007. Intestinal cholesterol transport proteins: an update and beyond. Curr. Opin. Lipidol. 18:310–318.
   PubMed Web of Science ®Google Scholar
• Mahajan, M. A., S. Das, H. Zhu, M. Tomic-Canic, and H. H. Samuels. 2004. The nuclear hormone receptor coactivator NRC is a pleiotropic modulator affecting growth, development, apoptosis, reproduction, and wound repair. Mol. Cell. Biol. 24:4994–5004.
   PubMedGoogle Scholar
• Mahajan, M. A., and H. H. Samuels. 2000. A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol. Cell. Biol. 20:5048–5063.
   PubMedGoogle Scholar
• Mahajan, M. A., and H. H. Samuels. 2005. Nuclear hormone receptor coregulator: role in hormone action, metabolism, growth, and development. Endocr. Rev. 26:583–597.
   PubMed Web of Science ®Google Scholar
• Mak, H. Y., S. Hoare, P. M. Henttu, and M. G. Parker. 1999. Molecular determinants of the estrogen receptor-coactivator interface. Mol. Cell. Biol. 19:3895–3903.
   PubMedGoogle Scholar
• McInerney, E. M., D. W. Rose, S. E. Flynn, S. Westin, T. M. Mullen, A. Krones, J. Inostroza, J. Torchia, R. T. Nolte, N. Assa-Munt, M. V. Milburn, C. K. Glass, and M. G. Rosenfeld. 1998. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 12:3357–3368.
   PubMed Web of Science ®Google Scholar
• McKenna, N. J., and B. W. O'Malley. 2002. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108:465–474.
   PubMed Web of Science ®Google Scholar
• Mussi, P., L. Liao, S. E. Park, P. Ciana, A. Maggi, B. S. Katzenellenbogen, J. Xu, and B. W. O'Malley. 2006. Haploinsufficiency of the corepressor of estrogen receptor activity (REA) enhances estrogen receptor function in the mammary gland. Proc. Natl. Acad. Sci. USA 103:16716–16721.
   PubMedGoogle Scholar
• Oberkofler, H., E. Schraml, F. Krempler, and W. Patsch. 2003. Potentiation of liver X receptor transcriptional activity by peroxisome-proliferator-activated receptor gamma co-activator 1 alpha. Biochem. J. 371:89–96.
   PubMedGoogle Scholar
• O'Malley, B. W. 2007. Coregulators: from whence came these “master genes.” Mol. Endocrinol. 21:1009–1013.
   PubMed Web of Science ®Google Scholar
• Peet, D. J., S. D. Turley, W. Ma, B. A. Janowski, J. M. Lobaccaro, R. E. Hammer, and D. J. Mangelsdorf. 1998. Cholesterol and bile acid metabolism are impaired in mice lacking the nuclear oxysterol receptor LXR alpha. Cell 93:693–704.
   PubMed Web of Science ®Google Scholar
• Qi, C., P. Kashireddy, Y. T. Zhu, S. M. Rao, and Y. J. Zhu. 2004. Null mutation of peroxisome proliferator-activated receptor-interacting protein in mammary glands causes defective mammopoiesis. J. Biol. Chem. 279:33696–33701.
   PubMedGoogle Scholar
• Repa, J. J., G. Liang, J. Ou, Y. Bashmakov, J. M. Lobaccaro, I. Shimomura, B. Shan, M. S. Brown, J. L. Goldstein, and D. J. Mangelsdorf. 2000. Regulation of mouse sterol regulatory element-binding protein-1c gene (SREBP-1c) by oxysterol receptors, LXRα and LXRβ. Genes Dev. 14:2819–2830.
   PubMed Web of Science ®Google Scholar
• Repa, J. J., and D. J. Mangelsdorf. 2000. The role of orphan nuclear receptors in the regulation of cholesterol homeostasis. Annu. Rev. Cell Dev. Biol. 16:459–481.
   PubMed Web of Science ®Google Scholar
• Rosenfeld, M. G., V. V. Lunyak, and C. K. Glass. 2006. Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response. Genes Dev. 20:1405–1428.
   PubMed Web of Science ®Google Scholar
• Shiau, A. K., D. Barstad, P. M. Loria, L. Cheng, P. J. Kushner, D. A. Agard, and G. L. Greene. 1998. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95:927–937.
   PubMed Web of Science ®Google Scholar
• Ulven, S. M., K. T. Dalen, J. A. Gustafsson, and H. I. Nebb. 2005. LXR is crucial in lipid metabolism. Prostaglandins Leukot. Essent. Fatty Acids 73:59–63.
   PubMedGoogle Scholar
• Unno, A., I. Takada, S. Takezawa, H. Oishi, A. Baba, T. Shimizu, A. Tokita, J. Yanagisawa, and S. Kato. 2005. TRRAP as a hepatic coactivator of LXR and FXR function. Biochem. Biophys. Res. Commun. 327:933–938.
   PubMedGoogle Scholar
• Xu, J. 2005. Preparation, culture, and immortalization of mouse embryonic fibroblasts, p. 28.1.1–28.1.8. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 5. Wiley, Hoboken, NJ.
   Google Scholar
• Xu, J., and Q. Li. 2003. Review of the in vivo functions of the p160 steroid receptor coactivator family. Mol. Endocrinol. 17:1681–1692.
   PubMed Web of Science ®Google Scholar
• Xu, J., L. Liao, G. Ning, H. Yoshida-Komiya, C. Deng, and B. W. O'Malley. 2000. The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development. Proc. Natl. Acad. Sci. USA 97:6379–6384.
   PubMedGoogle Scholar
• Yeom, S. Y., G. H. Kim, C. H. Kim, H. D. Jung, S. Y. Kim, J. Y. Park, Y. K. Pak, D. K. Rhee, S. Q. Kuang, J. Xu, D. J. Han, D. K. Song, J. W. Lee, K. U. Lee, and S. W. Kim. 2006. Regulation of insulin secretion and beta-cell mass by activating signal cointegrator 2. Mol. Cell. Biol. 26:4553–4563.
   PubMedGoogle Scholar
• Yokode, M., R. E. Hammer, S. Ishibashi, M. S. Brown, and J. L. Goldstein. 1990. Diet-induced hypercholesterolemia in mice: prevention by overexpression of LDL receptors. Science 250:1273–1275.
   PubMed Web of Science ®Google Scholar
• Yoshikawa, T., H. Shimano, M. Amemiya-Kudo, N. Yahagi, A. H. Hasty, T. Matsuzaka, H. Okazaki, Y. Tamura, Y. Iizuka, K. Ohashi, J. Osuga, K. Harada, T. Gotoda, S. Kimura, S. Ishibashi, and N. Yamada. 2001. Identification of liver X receptor-retinoid X receptor as an activator of the sterol regulatory element-binding protein 1c gene promoter. Mol. Cell. Biol. 21:2991–3000.
   PubMed Web of Science ®Google Scholar
• Zelcer, N., and P. Tontonoz. 2006. Liver X receptors as integrators of metabolic and inflammatory signaling. J. Clin. Investig. 116:607–614.
   PubMed Web of Science ®Google Scholar
• Zhang, H., S. Q. Kuang, L. Liao, S. Zhou, and J. Xu. 2004. Haploid inactivation of the amplified-in-breast cancer 3 coactivator reduces the inhibitory effect of peroxisome proliferator-activated receptor gamma and retinoid X receptor on cell proliferation and accelerates polyoma middle-T antigen-induced mammary tumorigenesis in mice. Cancer Res. 64:7169–7177.
   PubMedGoogle Scholar
• Zhang, H., L. Liao, S. Q. Kuang, and J. Xu. 2003. Spatial distribution of the messenger ribonucleic acid and protein of the nuclear receptor coactivator, amplified in breast cancer-3, in mice. Endocrinology 144:1435–1443.
   PubMedGoogle Scholar
• Zhang, Y., J. J. Repa, K. Gauthier, and D. J. Mangelsdorf. 2001. Regulation of lipoprotein lipase by the oxysterol receptors, LXRα and LXRβ. J. Biol. Chem. 276:43018–43024.
   PubMed Web of Science ®Google Scholar
• Zhu, Y., L. Kan, C. Qi, Y. S. Kanwar, A. V. Yeldandi, M. S. Rao, and J. K. Reddy. 2000. Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR. J. Biol. Chem. 275:13510–13516.
   PubMed Web of Science ®Google Scholar
• Zhu, Y. J., S. E. Crawford, V. Stellmach, R. S. Dwivedi, M. S. Rao, F. J. Gonzalez, C. Qi, and J. K. Reddy. 2003. Coactivator PRIP, the peroxisome proliferator-activated receptor-interacting protein, is a modulator of placental, cardiac, hepatic, and embryonic development. J. Biol. Chem. 278:1986–1990.
   PubMedGoogle Scholar