Competitive Cofactor Recruitment by Orphan Receptor Hepatocyte Nuclear Factor 4α1: Modulation by the F Domain

REFERENCES

• Apriletti, J. W., R. C. Ribeiro, R. L. Wagner, W. Feng, P. Webb, P. J. Kushner, B. L. West, S. Nilsson, T. S. Scanlan, R. J. Fletterick, and J. D. Baxter. 1998. Molecular and structural biology of thyroid hormone receptors. Clin. Exp. Pharmacol. Physiol. Suppl. 25: S2–S11.
   PubMedGoogle Scholar
• Bevan, C. L., S. Hoare, F. Claessens, D. M. Heery, and M. G. Parker. 1999. The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1. Mol. Cell. Biol. 19: 8383–8392.
   PubMed Web of Science ®Google Scholar
• Bogan, A. A., Q. Dallas-Yang, M. D. Ruse, Jr., Y. Maeda, G. Jiang, L. Nepomuceno, T. S. Scanlan, F. E. Cohen, and F. M. Sladek. 2000. Analysis of protein dimerization and ligand binding of orphan receptor HNF4alpha. J. Mol. Biol. 302: 831–851.
   PubMed Web of Science ®Google Scholar
• Burke, L. J., and A. Baniahmad. 2000. Co-repressors 2000. FASEB J. 14: 1876–1888.
   Google Scholar
• Chakravarti, D., V. J. LaMorte, M. C. Nelson, T. Nakajima, I. G. Schulman, H. Juguilon, M. Montminy, and R. M. Evans. 1996. Role of CBP/P300 in nuclear receptor signalling. Nature 383: 99–103.
   PubMed Web of Science ®Google Scholar
• Chen, J. D., and R. M. Evans. 1995. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377: 454–457.
   PubMed Web of Science ®Google Scholar
• Cheung, P., C. D. Allis, and P. Sassone-Corsi. 2000. Signaling to chromatin through histone modifications. Cell 103: 263–271.
   PubMed Web of Science ®Google Scholar
• Dallas-Yang, Q., G. Jiang, and F. M. Sladek. 1998. Avoiding false positives in colony PCR. BioTechniques 24: 580–582.
   PubMedGoogle Scholar
• Dell, H., and M. Hadzopoulou-Cladaras. 1999. CREB binding protein is a transcriptional coactivator for hepatocyte nuclear factor-4 and enhances apolipoprotein gene expression. J. Biol. Chem. 274: 9013–9021.
   PubMed Web of Science ®Google Scholar
• Ding, X. F., C. M. Anderson, H. Ma, H. Hong, R. M. Uht, P. J. Kushner, and M. R. Stallcup. 1998. Nuclear receptor-binding sites of coactivators glucocorticoid receptor interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1): multiple motifs with different binding specificities. Mol. Endocrinol. 12: 302–313.
   PubMedGoogle Scholar
• Dowell, P., J. E. Ishmael, D. Avram, V. J. Peterson, D. J. Nevrivy, and M. Leid. 1999. Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein. J. Biol. Chem. 274: 15901–15907.
   PubMedGoogle Scholar
• Eckner, R., M. E. Ewen, D. Newsome, M. Gerdes, J. A. DeCaprio, J. B. Lawrence, and D. M. Livingston. 1994. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 8: 869–884.
   PubMed Web of Science ®Google Scholar
• Freedman, L. P. 1999. Increasing the complexity of coactivation in nuclear receptor signaling. Cell 97: 5–8.
   PubMed Web of Science ®Google Scholar
• Freedman, L. P. 1999. Strategies for transcriptional activation by steroid/nuclear receptors. J. Cell. Biochem. Suppl. 32-33: 103–109.
   Google Scholar
• Fu, M., C. Wang, A. T. Reutens, J. Wang, R. H. Angeletti, L. Siconolfi-Baez, V. Ogryzko, M. L. Avantaggiati, and R. G. Pestell. 2000. p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation. J. Biol. Chem. 275: 20853–20860.
   PubMed Web of Science ®Google Scholar
• Gelman, L., G. Zhou, L. Fajas, E. Raspé, J. C. Fruchart, and J. Auwerx. 1999. p300 interacts with the N- and C-terminal part of PPARgamma2 in a ligand-independent and -dependent manner, respectively. J. Biol. Chem. 274: 7681–7688.
   PubMed Web of Science ®Google Scholar
• Green, V. J., E. Kokkotou, and J. A. Ladias. 1998. Critical structural elements and multitarget protein interactions of the transcriptional activator AF-1 of hepatocyte nuclear factor 4. J. Biol. Chem. 273: 29950–29957.
   Google Scholar
• Hammer, G. D., I. Krylova, Y. Zhang, B. D. Darimont, K. Simpson, N. L. Weigel, and H. A. Ingraham. 1999. Phosphorylation of the nuclear receptor SF-1 modulates cofactor recruitment: integration of hormone signaling in reproduction and stress. Mol. Cell 3: 521–526.
   PubMed Web of Science ®Google Scholar
• Harish, S., T. Khanam, S. Mani, and P. Rangarajan. 2001. Transcriptional activation by hepatocyte nuclear factor-4 in a cell-free system derived from rat liver nuclei. Nucleic Acids Res. 29: 1047–1053.
   PubMedGoogle Scholar
• Heinzel, T., R. M. Lavinsky, T. M. Mullen, M. Söderstrom, C. D. Laherty, J. Torchia, W. M. Yang, G. Brard, S. D. Ngo, J. R. Davie, E. Seto, R. N. Eisenman, D. W. Rose, C. K. Glass, and M. G. Rosenfeld. 1997. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387: 43–48.
   PubMed Web of Science ®Google Scholar
• Hertz, R., J. Magenheim, I. Berman, and J. Bar-Tana. 1998. Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4alpha. Nature 392: 512–516.
   PubMed Web of Science ®Google Scholar
• Hong, S. H., G. David, C. W. Wong, A. Dejean, and M. L. Privalsky. 1997. SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia. Proc. Natl. Acad. Sci. USA 94: 9028–9033.
   PubMed Web of Science ®Google Scholar
• Hong, S. H., and M. L. Privalsky. 2000. The SMRT corepressor is regulated by a MEK-1 kinase pathway: inhibition of corepressor function is associated with SMRT phosphorylation and nuclear export. Mol. Cell. Biol. 20: 6612–6625.
   PubMed Web of Science ®Google Scholar
• Hörlein, A. J., A. M. Näär, T. Heinzel, J. Torchia, B. Gloss, R. Kurokawa, A. Ryan, Y. Kamei, M. Söderström, C. K. Glass, et al. 1995. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 377: 397–404.
   PubMed Web of Science ®Google Scholar
• Hsu, I. C., T. Tokiwa, W. Bennett, R. A. Metcalf, J. A. Welsh, T. Sun, and C. C. Harris. 1993. p53 gene mutation and integrated hepatitis B viral DNA sequences in human liver cancer cell lines. Carcinogenesis 14: 987–992.
   PubMed Web of Science ®Google Scholar
• Hu, X., and M. A. Lazar. 1999. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 402: 93–96.
   PubMed Web of Science ®Google Scholar
• Hu, X., Y. Li, and M. A. Lazar. 2001. Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors. Mol. Cell. Biol. 21: 1747–1758.
   PubMedGoogle Scholar
• Iyemere, V. P., N. H. Davies, and G. G. Brownlee. 1998. The activation function 2 domain of hepatic nuclear factor 4 is regulated by a short C-terminal proline-rich repressor domain. Nucleic Acids Res. 26: 2098–2104.
   PubMed Web of Science ®Google Scholar
• Jiang, G., L. Nepomuceno, K. Hopkins, and F. M. Sladek. 1995. Exclusive homodimerization of the orphan receptor hepatocyte nuclear factor 4 defines a new subclass of nuclear receptors. Mol. Cell. Biol. 15: 5131–5143.
   PubMed Web of Science ®Google Scholar
• Jiang, G., L. Nepomuceno, Q. Yang, and F. M. Sladek. 1997. Serine/threonine phosphorylation of orphan receptor hepatocyte nuclear factor 4. Arch. Biochem. Biophys. 340: 1–9.
   Google Scholar
• Jiang, G., and F. M. Sladek. 1997. The DNA binding domain of hepatocyte nuclear factor 4 mediates cooperative, specific binding to DNA and heterodimerization with the retinoid X receptor alpha. J. Biol. Chem. 272: 1218–1225.
   PubMedGoogle Scholar
• Knoepfler, P. S., and R. N. Eisenman. 1999. Sin meets NuRD and other tails of repression. Cell 99: 447–450.
   PubMed Web of Science ®Google Scholar
• Koh, S. S., D. Chen, Y. H. Lee, and M. R. Stallcup. 2001. Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. J. Biol. Chem. 276: 1089–1098.
   PubMed Web of Science ®Google Scholar
• Leff, T., K. Reue, A. Melian, H. Culver, and J. L. Breslow. 1989. A regulatory element in the ApoCIII promoter that directs hepatic specific transcription binds to proteins in expressing and nonexpressing cell types. J. Biol. Chem. 264: 16132–16137.
   PubMedGoogle Scholar
• Lemon, B. D., and L. P. Freedman. 1999. Nuclear receptor cofactors as chromatin remodelers. Curr. Opin. Genet. Dev. 9: 499–504.
   PubMedGoogle Scholar
• Li, H., C. Leo, D. J. Schroen, and J. D. Chen. 1997. Characterization of receptor interaction and transcriptional repression by the corepressor SMRT. Mol. Endocrinol. 11: 2025–2037.
   PubMedGoogle Scholar
• Lin, R. J., L. Nagy, S. Inoue, W. Shao, W. H. Miller, Jr., and R. M. Evans. 1998. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391: 811–814.
   PubMed Web of Science ®Google Scholar
• Maeda, Y., S. D. Seidel, G. Wei, X. Liu, and F. M. Sladek. 2002. Repression of hepatocyte nuclear factor 4α by tumor suppressor p53: involvement of the ligand binding domain and histone deacetylase activity. Mol. Endocrinol. 16: 402–410.
   PubMedGoogle Scholar
• Malik, S., W. Gu, W. Wu, J. Qin, and R. G. Roeder. 2000. The USA-derived transcriptional coactivator PC2 is a submodule of TRAP/SMCC and acts synergistically with other PCs. Mol. Cell 5: 753–760.
   PubMed Web of Science ®Google Scholar
• Malik, S., and S. K. Karathanasis. 1996. TFIIB-directed transcriptional activation by the orphan nuclear receptor hepatocyte nuclear factor 4. Mol. Cell. Biol. 16: 1824–1831.
   Google Scholar
• Mangelsdorf, D. J., U. Borgmeyer, R. A. Heyman, J. Y. Zhou, E. S. Ong, A. E. Oro, A. Kakizuka, and R. M. Evans. 1992. Characterization of three RXR genes that mediate the action of 9-cis retinoic acid. Genes Dev. 6: 329–344.
   PubMed Web of Science ®Google Scholar
• Mangelsdorf, D. J., C. Thummel, M. Beato, P. Herrlich, G. Schütz, K. Umesono, B. Blumberg, P. Kastner, M. Mark, P. Chambon, et al. 1995. The nuclear receptor superfamily: the second decade. Cell 83: 835–839.
   PubMed Web of Science ®Google Scholar
• Marmorstein, R. 2001. Protein modules that manipulate histone tails for chromatin regulation. Nat. Rev. Mol. Cell. Biol. 2: 422–432.
   PubMed Web of Science ®Google Scholar
• McKenna, N. J., J. Xu, Z. Nawaz, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1999. Nuclear receptor coactivators: multiple enzymes, multiple complexes, multiple functions. J. Steroid Biochem. Mol. Biol. 69: 3–12.
   PubMed Web of Science ®Google Scholar
• Nagy, L., H. Y. Kao, D. Chakravarti, R. J. Lin, C. A. Hassig, D. E. Ayer, S. L. Schreiber, and R. M. Evans. 1997. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89: 373–380.
   PubMed Web of Science ®Google Scholar
• Nagy, L., H. Y. Kao, J. D. Love, C. Li, E. Banayo, J. T. Gooch, V. Krishna, K. Chatterjee, R. M. Evans, and J. W. Schwabe. 1999. Mechanism of corepressor binding and release from nuclear hormone receptors. Genes Dev. 13: 3209–3216.
   PubMed Web of Science ®Google Scholar
• Nakhei, H., A. Lingott, I. Lemm, and G. U. Ryffel. 1998. An alternative splice variant of the tissue specific transcription factor HNF4alpha predominates in undifferentiated murine cell types. Nucleic Acids Res. 26: 497–504.
   PubMedGoogle Scholar
• Nuclear Receptor Nomenclature Committee. 1999. A unified nomenclature system for the nuclear receptor superfamily. Cell 97: 161–163.
   PubMed Web of Science ®Google Scholar
• Ogryzko, V. V., R. L. Schiltz, V. Russanova, B. H. Howard, and Y. Nakatani. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87: 953–959.
   PubMed Web of Science ®Google Scholar
• Onate, S. A., V. Boonyaratanakornkit, T. E. Spencer, S. Y. Tsai, M. J. Tsai, D. P. Edwards, and B. W. O'Malley. 1998. The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J. Biol. Chem. 273: 12101–12108.
   PubMed Web of Science ®Google Scholar
• Perissi, V., L. M. Staszewski, E. M. McInerney, R. Kurokawa, A. Krones, D. W. Rose, M. H. Lambert, M. V. Milburn, C. K. Glass, and M. G. Rosenfeld. 1999. Molecular determinants of nuclear receptor-corepressor interaction. Genes Dev. 13: 3198–3208.
   PubMed Web of Science ®Google Scholar
• Petrij, F., R. H. Giles, H. G. Dauwerse, J. J. Saris, R. C. Hennekam, M. Masuno, N. Tommerup, G. J. van Ommen, R. H. Goodman, D. J. Peters, et al. 1995. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature 376: 348–351.
   PubMed Web of Science ®Google Scholar
• Shibata, H., T. E. Spencer, S. A. Oñate, G. Jenster, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1997. Role of co-activators and co-repressors in the mechanism of steroid/thyroid receptor action. Recent Prog. Hormone Res. 52: 141–164.
   PubMedGoogle Scholar
• Sladek, F. M., Q. Dallas-Yang, and L. Nepomuceno. 1998. MODY1 mutation Q268X in hepatocyte nuclear factor 4alpha allows for dimerization in solution but causes abnormal subcellular localization. Diabetes 47: 985–990.
   PubMed Web of Science ®Google Scholar
• Sladek, F. M., M. D. Ruse, Jr., L. Nepomuceno, S. M. Huang, and M. R. Stallcup. 1999. Modulation of transcriptional activation and coactivator interaction by a splicing variation in the F domain of nuclear receptor hepatocyte nuclear factor 4α1. Mol. Cell. Biol. 19: 6509–6522.
   PubMed Web of Science ®Google Scholar
• Sladek, F. M., and S. D. Seidel. 2001. Hepatocyte nuclear factor 4α, p. 309–361. In T. Burris and E. R. B. McCabe (ed.), Nuclear receptors and genetic diseases. Academic Press, London., England.
   Google Scholar
• Sladek, F. M., W. M. Zhong, E. Lai, and J. E. Darnell, Jr. 1990. Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily. Genes Dev. 4: 2353–2365.
   PubMed Web of Science ®Google Scholar
• Sladek, R., and V. Giguère. 2000. Orphan nuclear receptors: an emerging family of metabolic regulators. Adv. Pharmacol. 47: 23–87.
   PubMedGoogle Scholar
• Soutoglou, E., N. Katrakili, and I. Talianidis. 2000. Acetylation regulates transcription factor activity at multiple levels. Mol. Cell 5: 745–751.
   PubMed Web of Science ®Google Scholar
• Spencer, T. E., G. Jenster, M. M. Burcin, C. D. Allis, J. Zhou, C. A. Mizzen, N. J. McKenna, S. A. Onate, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1997. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389: 194–198.
   PubMed Web of Science ®Google Scholar
• Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. K. Glass, and M. G. Rosenfeld. 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387: 677–684.
   PubMed Web of Science ®Google Scholar
• Tremblay, A., G. B. Tremblay, F. Labrie, and V. Giguère. 1999. Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1. Mol. Cell 3: 513–519.
   PubMed Web of Science ®Google Scholar
• Tsai, M. J., and B. W. O'Malley. 1994. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63: 451–486.
   PubMed Web of Science ®Google Scholar
• Tyler, J. K., and J. T. Kadonaga. 1999. The “dark side” of chromatin remodeling: repressive effects on transcription. Cell 99: 443–446.
   PubMed Web of Science ®Google Scholar
• Umesono, K., K. K. Murakami, C. C. Thompson, and R. M. Evans. 1991. Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell 65: 1255–1266.
   PubMed Web of Science ®Google Scholar
• Wang, J. C., J. M. Stafford, and D. K. Granner. 1998. SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4. J. Biol. Chem. 273: 30847–30850.
   Google Scholar
• Weigel, N. L., W. Bai, Y. Zhang, C. A. Beck, D. P. Edwards, and A. Poletti. 1995. Phosphorylation and progesterone receptor function. J. Steroid Biochem. Mol. Biol. 53: 509–514.
   PubMed Web of Science ®Google Scholar
• Weigel, N. L., and Y. Zhang. 1998. Ligand-independent activation of steroid hormone receptors. J. Mol. Med. 76: 469–479.
   PubMedGoogle Scholar
• Whitfield, G. K., P. W. Jurutka, C. A. Haussler, and M. R. Haussler. 1999. Steroid hormone receptors: evolution, ligands, and molecular basis of biologic function. J. Cell. Biochem. Suppl. 32-33: 110–122.
   Google Scholar
• Wong, C. W., and M. L. Privalsky. 1998. Transcriptional repression by the SMRT-mSin3 corepressor: multiple interactions, multiple mechanisms, and a potential role for TFIIB. Mol. Cell. Biol. 18: 5500–5510.
   PubMedGoogle Scholar
• Xu, L., C. K. Glass, and M. G. Rosenfeld. 1999. Coactivator and corepressor complexes in nuclear receptor function. Curr. Opin. Genet. Dev. 9: 140–147.
   PubMed Web of Science ®Google Scholar
• Yoh, S. M., and M. L. Privalsky. 2000. Resistance to thyroid hormone (RTH) syndrome reveals novel determinants regulating interaction of T3 receptor with corepressor. Mol. Cell. Endocrinol. 159: 109–124.
   PubMedGoogle Scholar
• Yoshida, E., S. Aratani, H. Itou, M. Miyagishi, M. Takiguchi, T. Osumu, K. Murakami, and A. Fukamizu. 1997. Functional association between CBP and HNF4 in trans-activation. Biochem. Biophys. Res. Commun. 241: 664–669.
   PubMedGoogle Scholar
• Zamir, I., J. Zhang, and M. A. Lazar. 1997. Stoichiometric and steric principles governing repression by nuclear hormone receptors. Genes Dev. 11: 835–846.
   PubMed Web of Science ®Google Scholar
• Zhang, J., X. Hu, and M. A. Lazar. 1999. A novel role for helix 12 of retinoid X receptor in regulating repression. Mol. Cell. Biol. 19: 6448–6457.
   PubMed Web of Science ®Google Scholar