Proteasomal Inhibition Enhances Glucocorticoid Receptor Transactivation and Alters Its Subnuclear Trafficking

REFERENCES

• Archer, T. K., M. G. Cordingley, R. G. Wolford, and G. L. Hager. 1991. Transcription factor access is mediated by accurately positioned nucleosomes on the mouse mammary tumor virus promoter. Mol. Cell. Biol. 11: 688–698.
   PubMed Web of Science ®Google Scholar
• Archer, T. K., B. J. Deroo, and C. J. Fryer. 1997. Chromatin modulation of glucocorticoid and progesterone receptor activity. Trends Endocrinol. Metab. 8: 384–390.
   PubMedGoogle Scholar
• Archer, T. K., P. Lefebvre, R. G. Wolford, and G. L. Hager. 1992. Transcription factor loading on the MMTV promoter: a bimodal mechanism for promoter activation. Science 255: 1573-1576. (Erratum, 256: 161.)
   PubMed Web of Science ®Google Scholar
• Archer, T. K., E. Zaniewski, M. L. Moyer, and S. K. Nordeen. 1994. The differential capacity of glucocorticoids and progestins to alter chromatin structure and induce gene expression in human breast cancer cells. Mol. Endocrinol. 8: 1154–1162.
   PubMedGoogle Scholar
• Baumann, C. T., H. Ma, R. Wolford, J. C. Reyes, P. Maruvada, C. Lim, P. M. Yen, M. R. Stallcup, and G. L. Hager. 2001. The glucocorticoid receptor interacting protein 1(GRIP1) localizes in discrete nuclear foci that associate with ND10 bodies and are enriched in components of the 26S proteasome. Mol. Endocrinol. 15: 485–500.
   PubMedGoogle Scholar
• Bellingham, D. L., M. Sar, and J. A. Cidlowski. 1992. Ligand-dependent down-regulation of stably transfected human glucocorticoid receptors is associated with the loss of functional glucocorticoid responsiveness. Mol. Endocrinol. 6: 2090–2102.
   PubMedGoogle Scholar
• Blagosklonny, M. V., W. G. An, G. Melillo, P. Nguyen, J. B. Trepel, and L. M. Neckers. 1999. Regulation of BRCA1 by protein degradation. Oncogene 18: 6460–6468.
   PubMedGoogle Scholar
• Bourgeois, S., and R. F. Newby. 1979. Correlation between glucocorticoid receptor and cytolytic response of murine lymphoid cell lines. Cancer Res. 39: 4749–4751.
   PubMedGoogle Scholar
• Campanero, M. R., and E. K. Flemington. 1997. Regulation of E2F through ubiquitin-proteasome-dependent degradation: stabilization by the pRB tumor suppressor protein. Proc. Natl. Acad. Sci. USA 94: 2221–2226.
   PubMed Web of Science ®Google Scholar
• Carey, K. L., S. A. Richards, K. M. Lounsbury, and I. G. Macara. 1996. Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the Ran/TC4 GTPase mediates an essential function independent of nuclear protein import. J. Cell Biol. 133: 985–996.
   PubMedGoogle Scholar
• Cato, A. C., and E. Wade. 1996. Molecular mechanisms of anti-inflammatory action of glucocorticoids. Bioessays 18: 371–378.
   PubMed Web of Science ®Google Scholar
• Chowdary, D. R., J. J. Dermody, K. K. Jha, and H. L. Ozer. 1994. Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol. Cell. Biol. 14: 1997–2003.
   PubMed Web of Science ®Google Scholar
• Connell, P., C. A. Ballinger, J. Jiang, Y. Wu, L. J. Thompson, J. Hohfeld, and C. Patterson. 2001. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3: 93–96.
   PubMed Web of Science ®Google Scholar
• Deroo, B. J., and T. K. Archer. 2001. Glucocorticoid receptor-mediated chromatin remodeling in vivo. Oncogene Rev. 20: 3039–3046.
   PubMedGoogle Scholar
• Ferdous, A., F. Gonzalez, L. Sun, T. Kodadek, and S. A. Johnston. 2001. The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II. Mol. Cell 7: 981–991.
   PubMed Web of Science ®Google Scholar
• Fryer, C. J., S. K. Nordeen, and T. K. Archer. 1998. Antiprogestins mediate differential effects on glucocorticoid receptor remodeling of chromatin structure J. Biol. Chem. 273: 1175–1183.
   Google Scholar
• Gehring, U., K. Mugele, and J. Ulrich. 1984. Cellular receptor levels and glucocorticoid responsiveness of lymphoma cells. Mol. Cell. Endocrinol. 36: 107–113.
   PubMed Web of Science ®Google Scholar
• He, D. C., J. A. Nickerson, and S. Penman. 1990. Core filaments of the nuclear matrix. J. Cell Biol. 110: 569–580.
   PubMed Web of Science ®Google Scholar
• Hicke, L. 2001. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell. Biol. 2: 195–201.
   PubMed Web of Science ®Google Scholar
• Kinyamu, H. K., C. J. Fryer, K. B. Horwitz, and T. K. Archer. 2000. The MMTV promoter adopts distinct chromatin structures in human breast cancer cells with and without glucocorticoid receptor. J. Biol. Chem. 275: 20061–20068.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Lee, D., and A. Goldberg. 1998. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8: 397.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• McKay, L. I., and J. A. Cidlowski. 1999. Molecular control of immune/inflammatory responses: interactions between nuclear factor-kappa B and steroid receptor-signaling pathways. Endocr. Rev. 20: 435–459.
   PubMed Web of Science ®Google Scholar
• McNally, J. G., W. G. Muller, D. Walker, R. Wolford, and G. L. Hager. 2000. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science 287: 1262–1265.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Mymryk, J. S., D. Berard, G. L. Hager, and T. K. Archer. 1995. Mouse mammary tumor virus chromatin in human breast cancer cells is constitutively hypersensitive and exhibits steroid hormone-independent loading of transcription factors in vivo. Mol. Cell. Biol. 15: 26–34.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Nordeen, S. K., B. Kuhnel, J. Lawler-Heavner, D. A. Barber, and D. P. Edwards. 1989. A quantitative comparison of dual control of a hormone response element by progestins and glucocorticoids in the same cell line. Mol. Endocrinol. 3: 1270–1278.
   PubMedGoogle Scholar
• Osburn, D. L., G. Shao, H. M. Seidel, and I. G. Schulman. 2001. Ligand-dependent degradation of retinoid X receptors does not require transcriptional activity or coactivator interactions. Mol. Cell. Biol. 21: 4909–4918.
   PubMed Web of Science ®Google Scholar
• Pennie, W. D., G. L. Hager, and C. L. Smith. 1995. Nucleoprotein structure influences the response of the mouse mammary tumor virus promoter to activation of the cyclic AMP signaling pathway. Mol. Cell. Biol. 15: 2125–2134.
   PubMedGoogle Scholar
• Poizat, C., V. Sartorelli, G. Chung, R. A. Kloner, and L. Kedes. 2000. Proteasome-mediated degradation of the coactivator p300 impairs cardiac transcription. Mol. Cell. Biol. 20: 8643–8654.
   PubMed Web of Science ®Google Scholar
• Reyes, J. C., C. Muchardt, and M. Yaniv. 1997. Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix. J. Cell Biol. 137: 263–274.
   PubMed Web of Science ®Google Scholar
• Salghetti, S. E., A. A. Caudy, J. G. Chenoweth, and W. P. Tansey. 2001. Regulation of transcriptional activation domain function by ubiquitin. Science 293: 1651–1653.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Santiago-Josefat, B., E. Pozo-Guisado, S. Mulero-Navarro, and P. M. Fernandez-Salguero. 2001. Proteasome inhibition induces nuclear translocation and transcriptional activation of the dioxin receptor in mouse embryo primary fibroblasts in the absence of xenobiotics. Mol. Cell. Biol. 21: 1700–1709.
   PubMedGoogle Scholar
• Scheinman, R. I., A. A. Beg, and A. S. Baldwin, Jr. 1993. NF-κB p100 (Lyt-10) is a component of H2TF1 and can function as an IκB-like molecule. Mol. Cell. Biol. 13: 6089–6101.
   PubMedGoogle Scholar
• Sheflin, L., B. Keegan, W. Zhang, and S. W. Spaulding. 2000. Inhibiting proteasomes in human HepG2 and LNCaP cells increases endogenous androgen receptor levels. Biochem. Biophys. Res. Commun. 276: 144–150.
   PubMed Web of Science ®Google Scholar
• Stenoien, D. L., K. Patel, M. G. Mancini, M. Dutertre, C. L. Smith, B. W. O'Malley, and M. A. Mancini. 2001. FRAP reveals that mobility of oestrogen receptor-alpha is ligand- and proteasome-dependent. Nat. Cell Biol. 3: 15–23.
   PubMed Web of Science ®Google Scholar
• Tang, Y., and D. B. DeFranco. 1996. ATP-dependent release of glucocorticoid receptors from the nuclear matrix. Mol. Cell. Biol. 16: 1989–2001.
   PubMedGoogle Scholar
• Thomas, D., and M. Tyers. 2000. Transcriptional regulation: kamikaze activators. Curr. Biol. 10: R341–R343.
   PubMed Web of Science ®Google Scholar
• Treier, M., L. M. Staszewski, and D. Bohmann. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78: 787–798.
   PubMed Web of Science ®Google Scholar
• van Steensel, B., G. Jenster, K. Damm, A. O. Brinkmann, and R. van Driel. 1995. Domains of the human androgen receptor and glucocorticoid receptor involved in binding to the nuclear matrix. J. Cell. Biochem. 57: 465–478.
   PubMedGoogle Scholar
• Wallace, A. D., and J. A. Cidlowski. 2001. Proteasome mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J. Biol. Chem. 276: 42714–42721.
   PubMed Web of Science ®Google Scholar
• Wallberg, A. E., A. Wright, and J. A. Gustafsson. 2001. Chromatin-remodeling complexes involved in gene activation by the glucocorticoid receptor. Vitam. Horm. 60: 75–122.
   Google Scholar
• Yang, J., and D. B. DeFranco. 1994. Differential roles of heat shock protein 70 in the in vitro nuclear import of glucocorticoid receptor and simian virus 40 large tumor antigen. Mol. Cell. Biol. 14: 5088–5098.
   PubMedGoogle Scholar
• Zhang, J., M. G. Guenther, R. W. Carthew, and M. A. Lazar. 1998. Proteasomal regulation of nuclear receptor corepressor-mediated repression. Genes Dev. 12: 1775–1780.
   PubMed Web of Science ®Google Scholar