12
Views
40
CrossRef citations to date
0
Altmetric
Transcriptional Regulation

Ligand-Dependent Degradation of Retinoid X Receptors Does Not Require Transcriptional Activity or Coactivator Interactions

, , &
Pages 4909-4918 | Received 13 Dec 2000, Accepted 01 May 2001, Published online: 28 Mar 2023

REFERENCES

  • Adam-Stitah, S., L. Penna, P. Chambon, and C. Rochette-Egly. 1999. Hyperphosphorylation of the retinoid X receptor alpha by activated c-Jun NH2-terminal kinases. J. Biol. Chem. 274:18932–18941.
  • Alarid, E. T., N. Bakopoulos, and N. Solodin. 1999. Proteasome-mediated proteolysis of estrogen receptor: a novel component in autologous down-regulation. Mol. Endocrinol. 13:1522–1534.
  • Boehm, M. F., L. Zhang, B. A. Badea, S. A. White, D. E. Mais, E. Berger, C. M. Suto, M. E. Goldman, and R. A. Heyman. 1994. Synthesis and structure-activity relationships of novel retinoid X receptor-selective retinoids. J. Med. Chem. 37:2930–2941.
  • Boehm, M. F., L. Zhang, L. Zhi, M. R. McClurg, E. Berger, M. Wagoner, D. E. Mais, C. M. Suto, P. J. A. Davies, R. A. Heyman, and A. M. Nadzan. 1995. Design and synthesis of potent retinoid X receptor selective ligands that induce apoptosis in leukemia cells. J. Med. Chem. 38:3146–3155.
  • Boudjelal, M., Z. Wang, J. J. Voorhees, and G. J. Fisher. 2000. Ubiquitin/proteasome pathway regulates levels of retinoic acid receptor gamma and retinoid X receptor alpha in human keratinocytes. Cancer Res. 60:2247–2252.
  • Bourguet, W., M. Ruff, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature 375:377–382.
  • Bourguet, W., V. Vivat, J. M. Wurtz, P. Chambon, H. Gronemeyer, and D. Moras. 2000. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol. Cell 5:289–298.
  • Canan Koch, S. S., L. J. Dardashti, J. J. Hebert, G. E. Croston, K. S. Flatten, R. A. Heyman, and A. M. Nadzan. 1996. Identification of the first retinoid X receptor homodimer antagonist. J. Med. Chem. 39:3229–3234.
  • Chen, J. D., and R. M. Evans. 1995. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377:454–457.
  • Chen, Z., J. Hagler, V. J. Palombella, F. Melandri, D. Scherer, D. Ballard, and T. Maniatis. 1995. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev. 9:1586–1597.
  • Clemm, D. L., L. Sherman, V. Boonyaratanakornkit, W. T. Schrader, N. L. Weigel, and D. P. Edwards. 2000. Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody. Mol. Endocrinol. 14:52–65.
  • Dace, A., L. Zhao, K. S. Park, T. Furuno, N. Takamura, M. Nakanishi, B. L. West, J. A. Hanover, and S. Cheng. 2000. Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors. Proc. Natl. Acad. Sci. USA 97:8985–8990.
  • Damm, K., R. A. Heyman, K. Umesono, and R. A. Evans. 1993. Functional inhibition of retinoic acid response by dominant negative retinoic receptor mutants. Proc. Natl. Acad. Sci. USA 90:2989–2993.
  • Darimont, B. D., R. L. Wagner, J. W. Apriletti, M. R. Stallcup, P. J. Kushner, J. D. Baxter, R. J. Fletterick, and K. R. Yamamoto. 1998. Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 12:3343–3356.
  • Davis, K. D., T. J. Berrodin, J. E. Stelmach, J. D. Winkler, and M. A. Lazar. 1994. Endogenous retinoid X receptors can function as hormone receptors in pituitary cells. Mol. Cell. Biol. 14:7105–7110.
  • Diehl, J. A., F. Zindy, and C. J. Sherr. 1997. Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes Dev. 11:957–972.
  • Egea, P. F., A. Mitschler, N. Rochel, M. Ruff, P. Chambon, and D. Moras. 2000. Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. EMBO J. 19:2592–2601.
  • Feng, W., R. C. Ribeiro, R. L. Wagner, H. Nguyen, J. W. Apriletti, R. J. Fletterick, J. D. Baxter, P. J. Kushner, and B. L. West. 1998. Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors. Science 280:1747–1749.
  • Forman, B. M., K. Umesono, J. Chen, and R. M. Evans. 1995. Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell 81:541–550.
  • Glass, C. K., R. Franco, C. Weinberger, V. R. Albert, R. M. Evans, and M. G. Rosenfeld. 1987. A c-erb-A binding site in rat growth hormone gene mediates trans-activation by thyroid hormone. Nature 329:738–741.
  • Glass, C. K., D. W. Rose, and M. G. Rosenfeld. 1997. Nuclear receptor coactivators. Curr. Opin. Cell Biol. 9:222–232.
  • Glass, C. K., and M. G. Rosenfeld. 2000. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 14:121–141.
  • Hauser, S., G. Adelmant, P. Sarraf, H. M. Wright, E. Mueller, and B. M. Spiegelman. 2000. Degradation of the peroxisome proliferator-activated receptor gamma is linked to ligand-dependent activation. J. Biol. Chem. 275:18527–18533.
  • 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.
  • Hochstrasser, M., and A. Varshavsky. 1990. In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor. Cell 61:697–708.
  • Hu, X., and M. A. Lazar. 1999. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 402:93–96.
  • Hunter, T.. 1997. Oncoprotein networks. Cell 88:333–346.
  • Kaiser, P., K. Flick, C. Wittenberg, and S. I. Reed. 2000. Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCF(Met30)-mediated inactivation of the transcription factor Met4. Cell 102:303–314.
  • Keidel, S., P. LeMotte, and C. Apfel. 1994. Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping. Mol. Cell. Biol. 14:287–298.
  • Kim, T. K., and T. Maniatis. 1996. Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science 273:1717–1719.
  • Kinzler, K. W., and B. Vogelstein. 1996. Lessons from hereditary colorectal cancer. Cell 87:159–170.
  • Kopf, E., J. L. Plassat, V. Vivat, H. de The, P. Chambon, and C. Rochette-Egly. 2000. Dimerization with RXRs and phosphorylation modulate the retinoic acid- induced degradation of RARα and RARγ and through the ubiquitin-proteasome pathway. J.Biol. Chem.
  • Kurokawa, R., J. DiRenzo, M. Boehm, J. Sugarman, B. Gloss, M. G. Rosenfeld, R. A. Heyman, and C. K. Glass. 1994. Regulation of retinoid signalling by receptor polarity and allosteric control of ligand binding. Nature 371:528–531.
  • Lala, D. S., R. Mukherjee, I. G. Schulman, S. S. Canan-Koch, L. J. Dardashti, A. M. Nadzan, G. E. Croston, R. M. Evans, and R. A. Heyman. 1996. Activation of specific RXR heterodimers by an antagonist of RXR homodimers. Nature 383:450–453.
  • Lange, C. A., T. Shen, and K. B. Horwitz. 2000. Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome. Proc. Natl. Acad. Sci. USA 97:1032–1037.
  • Leid, M.. 1994. Ligand-induced alteration of the protease sensitivity of retinoid X receptorα. J. Biol. Chem. 269:14175–14181.
  • Lonard, D. M., Z. Nawaz, C. L. Smith, and B. W. O'Malley. 2000. The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation. Mol. Cell 5:939–948.
  • 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.
  • Mangelsdorf, D. J., and R. M. Evans. 1995. The RXR heterodimers and orphan receptors. Cell 83:841–850.
  • Mangelsdorf, D. J., C. Thummel, M. Beato, P. Herrlich, G. Schutz, K. Umesono, P. Kastner, M. Mark, P. Chambon, and R. M. Evans. 1995. The nuclear receptor superfamily: the second decade. Cell 83:835–839.
  • 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.
  • Molinari, E., M. Gilman, and S. Natesan. 1999. Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo. EMBO J 18:6439–6447.
  • Moras, D., and H. Gronemeyer. 1998. The nuclear receptor ligand-binding domain: structure and function. Curr. Opin. Cell Biol. 10:384–391.
  • 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.
  • Nawaz, Z., D. M. Lonard, A. P. Dennis, C. L. Smith, and B. W. O'Malley. 1999. Proteasome-dependent degradation of the human estrogen receptor. Proc. Natl. Acad. Sci. USA 96:1858–1862.
  • Nolte, R. T., G. B. Wisely, S. Westin, J. E. Cobb, M. H. Lambert, R. Kurokawa, M. G. Rosenfeld, T. M. Willson, C. K. Glass, and M. V. Milburn. 1998. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature 395:137–143.
  • Nomura, Y., T. Nagaya, Y. Hayashi, F. Kambe, and H. Seo. 1999. 9-cis-Retinoic acid decreases the level of its cognate receptor, retinoid X receptor, through acceleration of the turnover. Biochem. Biophys. Res. Commun. 260:729–733.
  • Orford, K., C. Crockett, J. P. Jensen, A. M. Weissman, and S. W. Byers. 1997. Serine phosphorylation-regulated ubiquitination and degradation of beta-catenin. J. Biol. Chem. 272:24735–24738.
  • 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.
  • Radhakrishnan, I., G. C. Perez-Alvarado, D. Parker, H. J. Dyson, M. R. Montminy, and P. E. Wright. 1997. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91:741–752.
  • Renaud, J.-P., N. Rochel, M. Ruff, V. Vivat, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378:681–689.
  • Salghetti, S. E., M. Muratani, H. Wijnen, B. Futcher, and W. P. Tansey. 2000. Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis. Proc. Natl. Acad. Sci. USA 97:3118–3123.
  • Schreiber, E., P. Matthias, M. M. Muller, and W. Schaffner. 1989. Rapid detection of octamer binding proteins with ‘mini-extracts’, prepared from a small number of cells. Nucleic Acids Res. 17:6419
  • Schulman, I. G., D. Chakravarti, H. Juguilon, A. Romo, and R. M. Evans. 1995. Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation. Proc. Natl. Acad. Sci. USA 92:8288–8292.
  • Schulman, I. G., H. Juguilon, and R. M. Evans. 1996. Activation and repression by nuclear hormone receptors: hormone modulates an equilibrium between active and repressive states. Mol. Cell. Biol. 16:3807–3818.
  • Schulman, I. G., C. Li, J. W. R. Schwabe, and R. M. Evans. 1997. The phantom ligand effect: allosteric control of transcription by the retinoid X receptor. Genes Dev. 11:299–308.
  • Schulman, I. G., G. Shao, and R. A. Heyman. 1998. Transactivation by retinoid X receptor-peroxisome proliferator-activated receptor gamma (PPARγ) heterodimers: intermolecular synergy requires only the PPARγ hormone-dependent activation function. Mol. Cell. Biol. 18:3483–3494.
  • Shao, G., R. A. Heyman, and I. G. Schulman. 2000. Three amino acids specify coactivator choice by retinoid X receptors. Mol. Endocrinol. 14:1198–1209.
  • 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.
  • Uesugi, M., O. Nyanguile, H. Lu, A. J. Levine, and G. L. Verdine. 1997. Induced alpha helix in the VP16 activation domain upon binding to a human TAF. Science 277:1310–1313.
  • Umesono, K., V. Giguere, C. K. Glass, M. G. Rosenfeld, and R. M. Evans. 1988. Retinoic acid and thyroid hormone induce gene expression through a common responsive element. Nature 336:262–265.
  • Weinberg, R. A.. 1996. How cancer arises. Sci. Am. 275:62–70.
  • Wen, D. X., Y. F. Xu, D. E. Mais, M. E. Goldman, and D. P. McDonnell. 1994. The A and B isoforms of the human progesterone receptor operate through distinct signaling pathways within target cells. Mol. Cell. Biol. 14:8356–8364.
  • Westin, S., R. Kurokawa, R. T. Nolte, G. B. Wisely, E. M. McInerney, D. W. Rose, M. V. Milburn, M. G. Rosenfeld, and C. K. Glass. 1998. Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators. Nature 395:199–202.
  • Wiebel, F. F., and J.-A. Gustafsson. 1997. Heterodimeric interaction between retinoid X receptor α and orphan nuclear receptor OR1 reveals dimerization-induced activation as a novel mechanism of nuclear receptor activation. Mol. Cell. Biol. 17:3977–3986.
  • Willhite, C. C., M. I. Dawson, and U. Reichert. 1996. Receptor-selective retinoid agonists and teratogenic activity. Drug Metab. Rev. 28:105–119.
  • Won, K. A., and S. I. Reed. 1996. Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J 15:4182–4193.
  • Wurtz, J.-M., W. Bourguet, J.-P. Renaud, V. Vivat, P. Chambon, D. Moras, and H. Gronemeyer. 1996. A canonical structure for the ligand-binding domain of nuclear receptors. Nat. Struct. Biol. 3:87–94.
  • 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.
  • Zhu, J., M. Gianni, E. Kopf, N. Honore, M. Chelbi-Alix, M. Koken, F. Quignon, C. Rochette-Egly, and H. de The. 1999. Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RARα) and oncogenic RARα fusion proteins. Proc. Natl. Acad. Sci. USA 96:14807–14812.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.