Cofilin 1 Is Revealed as an Inhibitor of Glucocorticoid Receptor by Analysis of Hormone-Resistant Cells

REFERENCES

• Abel, A., Wochnik G., Rüegg J., Rouyer A., Holsboer F., and Rein T.. 2002. Activity of the glucocorticoid receptor in G2 and mitosis. Mol. Endocrinol. 16:1352–1366.
   PubMedGoogle Scholar
• Bamburg, J. R., and Wiggan O. P.. 2002. ADF/cofilin and actin dynamics in disease. Trends Cell Biol. 12:598–605.
   PubMed Web of Science ®Google Scholar
• Beato, M., Herrlich P., and Schütz G.. 1995. Steroid hormone receptors: many actors in search of a plot. Cell 83:851–857.
   PubMed Web of Science ®Google Scholar
• Bonovich, M. T., List H. J., Zhang S., Danielsen M., and Riegel A. T.. 1998. Identification of glucocorticoid receptor domains necessary for transcriptional activation of the mouse mammary tumor virus promoter integrated in the genome. Exp. Cell Res. 239:454–462.
   PubMedGoogle Scholar
• Brinkmann, A. O. 1994. Steroid hormone receptors: activators of gene transcription. J. Pediatr. Endocrinol. 7:275–282.
   PubMed Web of Science ®Google Scholar
• Carlier, M. F. 1998. Control of actin dynamics. Curr. Opin. Cell Biol. 10:45–51.
   PubMedGoogle Scholar
• De Kloet, E. R., Oitzl M. S., and Joels M.. 1993. Functional implications of brain corticosteroid receptor diversity. Cell. Mol. Neurobiol. 13:433–455.
   PubMed Web of Science ®Google Scholar
• De Martino, M. U., Bhattachryya N., Alesci S., Ichijo T., Chrousos G. P., and Kino T.. 2004. The glucocorticoid receptor (GR) and the orphan nuclear receptor chicken ovalbumin upstream promoter-transcription factor II (COUP-TFII) interact with and mutually affect each other's transcriptional activities: implications for intermediary metabolism. Mol. Endocrinol. 18:820–833.
   PubMedGoogle Scholar
• DeRijk, R., and Sternberg E. M.. 1997. Corticosteroid resistance and disease. Ann. Med. 29:79–82.
   PubMed Web of Science ®Google Scholar
• Dos Remedios, C., Chhabra D., Kekic M., Dedova I. V., Tsubakihara M., Berry D. A., and Nosworthy N. J.. 2003. Actin binding proteins: regulation of cytoskeletal microfilaments. Physiol. Rev. 83:433–473.
   PubMed Web of Science ®Google Scholar
• Evans-Storms, R. B., and Cidlowski J. A.. 1995. Regulation of apoptosis by steroid hormones. J. Steroid Biochem. Mol. Biol. 53:1–8.
   PubMedGoogle Scholar
• Feldker, D. E., Datson N. A., Veenema A. H., Meulmeester E., De Kloet E. R., and Vreugdenhil E.. 2003. Serial analysis of gene expression predicts structural differences in hippocampus of long attack latency and short attack latency mice. Eur. J. Neurosci. 17:379–387.
   PubMedGoogle Scholar
• Galigniana, M. D., Scruggs J. L., Herrington J., Welsh M. J., Carter-Su C., Housley P. R., and Pratt W. B.. 1998. Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton. Mol. Endocrinol. 12:1903–1913.
   PubMedGoogle Scholar
• Göttlicher, M., Heck S., Doucas V., Wade E., Kullmann M., Cato A. C., Evans R. M., and Herrlich P.. 1996. Interaction of the Ubc9 human homologue with c-Jun and with the glucocorticoid receptor. Steroids 61:257–262.
   PubMedGoogle Scholar
• Grove, J. R., Dieckmann B. S., Schroer T. A., and Ringold G. M.. 1980. Isolation of glucocorticoid-unresponsive rat hepatoma cells by fluorescence-activated cell sorting. Cell 21:47–56.
   PubMedGoogle Scholar
• Harrison, R. W., Lippman S. S., and VerHoeven R.. 1995. Selection of glucocorticoid-resistant mutations from an AtT-20 cell line containing a glucocorticoid-regulated selectable transgene. Biochem. Biophys. Res. Commun. 209:18–24.
   PubMedGoogle Scholar
• Herr, A., Wochnik G. M., Rosenhagen M. C., Holsboer F., and Rein T.. 2000. Rifampicin is not an activator of the glucocorticoid receptor. Mol. Pharmacol. 57:732–737.
   PubMedGoogle Scholar
• Hittelman, A. B., Burakov D., Iñiguez-Lluh J. A., Freedman L. P., and Garabedian M. J.. 1999. Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins. EMBO J. 18:5380–5388.
   PubMed Web of Science ®Google Scholar
• Hollenberg, S. M., and Evans R. M.. 1988. Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell 55:899–906.
   PubMed Web of Science ®Google Scholar
• Hong, H., Kohli K., Trivedi A., Johnson D. L., and Stallcup M. R.. 1996. GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc. Natl. Acad. Sci. USA 93:4948–4952.
   PubMedGoogle Scholar
• Hulkko, S. M., Wakui H., and Zilliacus J.. 2000. The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function. Biochem. J. 349:885–893.
   PubMedGoogle Scholar
• Hutchison, K. A., Dittmar K. D., Czar M. J., and Pratt W. B.. 1994. Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90. J. Biol. Chem. 269:5043–5049.
   PubMed Web of Science ®Google Scholar
• Iida, K., Matsumoto S., and Yahara I.. 1992. The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Struct. Funct. 17:39–46.
   PubMed Web of Science ®Google Scholar
• Jonat, C., Rahmsdorf H. J., Park K. K., Cato A. C., Gebel S., Ponta H., and Herrlich P.. 1990. Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone. Cell 62:1189–1204.
   PubMed Web of Science ®Google Scholar
• Karin, M. 1998. New twists in gene regulation by glucocorticoid receptor: is DNA binding dispensable? Cell 93:487–490.
   PubMed Web of Science ®Google Scholar
• Karin, M., Haslinger A., Heguy A., Dietlin T., and Imbra R.. 1987. Transcriptional control mechanisms which regulate the expression of human metallothionein genes. Experientia Suppl. 52:401–405.
   PubMedGoogle Scholar
• Lee, H. L., and Archer T. K.. 1998. Prolonged glucocorticoid exposure dephosphorylates histone H1 and inactivates the MMTV promoter. EMBO J. 17:1454–1466.
   PubMedGoogle Scholar
• Lee, S., Duncan K. A., Chou H., Chen D., Kohli K., Huang C. F., and Stallcup M. R.. 1995. A somatic cell genetic method for identification of untargeted mutations in the glucocorticoid receptor that cause hormone binding deficiencies. Mol. Endocrinol. 9:826–837.
   PubMedGoogle Scholar
• Li, X., Commane M., Burns C., Vithalani K., Cao Z., and Stark G. R.. 1999. Mutant cells that do not respond to interleukin-1 (IL-1) reveal a novel role for IL-1 receptor-associated kinase. Mol. Cell. Biol. 19:4643–4652.
   PubMedGoogle Scholar
• Liu, J., and DeFranco D. B.. 1999. Chromatin recycling of glucocorticoid receptors: implications for multiple roles of heat shock protein 90. Mol. Endocrinol. 13:355–365.
   PubMed Web of Science ®Google Scholar
• Makino, Y., Okamoto K., Yoshikawa N., Aoshima M., Hirota K., Yodoi J., Umesono K., Makino I., and Tanaka H.. 1996. Thioredoxin: a redox-regulating cellular cofactor for glucocorticoid hormone action. Cross talk between endocrine control of stress response and cellular antioxidant defense system. J. Clin. Investig. 98:2469–2477.
   PubMed Web of Science ®Google Scholar
• McGough, A., Pope B., Chiu W., and Weeds A.. 1997. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138:771–781.
   PubMed Web of Science ®Google Scholar
• McKendry, R., John J., Flavell D., Muller M., Kerr I. M., and Stark G. R.. 1991. High-frequency mutagenesis of human cells and characterization of a mutant unresponsive to both alpha and gamma interferons. Proc. Natl. Acad. Sci. USA 88:11455–11459.
   PubMed Web of Science ®Google Scholar
• Miyata, Y., and Yahara I.. 1991. Cytoplasmic 8 S glucocorticoid receptor binds to actin filaments through the 90-kDa heat shock protein moiety. J. Biol. Chem. 266:8779–8783.
   PubMedGoogle Scholar
• Moon, A., and Drubin D. G.. 1995. The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol. Biol. Cell 6:1423–1431.
   PubMedGoogle Scholar
• Moriyama, K., Iida K., and Yahara I.. 1996. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1:73–86.
   PubMed Web of Science ®Google Scholar
• Nebl, G., Meuer S. C., and Samstag Y.. 1996. Dephosphorylation of serine 3 regulates nuclear translocation of cofilin. J. Biol. Chem. 271:26276–26280.
   PubMed Web of Science ®Google Scholar
• Nishida, E., Maekawa S., and Sakai H.. 1984. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry 23:5307–5313.
   PubMed Web of Science ®Google Scholar
• Oren, A., Herschkovitz A., Ben-Dror I., Holdengreber V., Ben-Shaul Y., Seger R., and Vardimon L.. 1999. The cytoskeletal network controls c-Jun expression and glucocorticoid receptor transcriptional activity in an antagonistic and cell-type-specific manner. Mol. Cell. Biol. 19:1742–1750.
   PubMedGoogle Scholar
• Pellegrini, S., John J., Shearer M., Kerr I. M., and Stark G. R.. 1989. Use of a selectable marker regulated by alpha interferon to obtain mutations in the signaling pathway. Mol. Cell. Biol. 9:4605–4612.
   PubMedGoogle Scholar
• Posern, G., Sotiropoulos A., and Treisman R.. 2002. Mutant actins demonstrate a role for unpolymerized actin in control of transcription by serum response factor. Mol. Biol. Cell 13:4167–4178.
   PubMedGoogle Scholar
• Pratt, W. B., Silverstein A. M., and Galigniana M. D.. 1999. A model for the cytoplasmic trafficking of signalling proteins involving the hsp90-binding immunophilins and p50cdc37. Cell. Signal. 11:839–851.
   PubMed Web of Science ®Google Scholar
• Rabindran, S. K., Danielsen M., Firestone G. L., and Stallcup M. R.. 1987. Glucocorticoid-dependent maturation of viral proteins in mouse lymphoma cells: isolation of defective and hormone-independent cell variants. Somat. Cell Mol. Genet. 13:131–143.
   PubMedGoogle Scholar
• Robyr, D., Wolffe A. P., and Wahli W.. 2000. Nuclear hormone receptor coregulators in action: diversity for shared tasks. Mol. Endocrinol. 14:329–347.
   PubMedGoogle Scholar
• Schule, R., Rangarajan P., Kliewer S., Ransone L. J., Bolado J., Yang N., Verma I. M., and Evans R. M.. 1990. Functional antagonism between oncoprotein c-Jun and the glucocorticoid receptor. Cell 62:1217–1226.
   PubMed Web of Science ®Google Scholar
• Shibuya, T., and Morimoto K.. 1993. A review of the genotoxicity of 1-ethyl-1-nitrosourea. Mutat. Res. 297:3–38.
   PubMed Web of Science ®Google Scholar
• Sitcheran, R., Emter R., Kralli A., and Yamamoto K. R.. 2000. A genetic analysis of glucocorticoid receptor signaling. Identification and characterization of ligand-effect modulators in Saccharomyces cerevisiae. Genetics 156:963–972.
   PubMedGoogle Scholar
• Smith, C. L., Htun H., Wolford R. G., and Hager G. L.. 1997. Differential activity of progesterone and glucocorticoid receptors on mouse mammary tumor virus templates differing in chromatin structure. J. Biol. Chem. 272:14227–14235.
   PubMedGoogle Scholar
• Taft, S. A., Liber H. L., and Skopek T. R.. 1994. Mutational spectrum of ICR-191 at the hprt locus in human lymphoblastoid cells. Environ. Mol. Mutagen. 23:96–100.
   PubMedGoogle Scholar
• Tang, Y., and DeFranco D. B.. 1996. ATP-dependent release of glucocorticoid receptors from the nuclear matrix. Mol. Cell. Biol. 16:1989–2001.
   PubMedGoogle Scholar
• Vacchio, M. S., Ashwell J. D., and King L. B.. 1998. A positive role for thymus-derived steroids in formation of the T-cell repertoire. Ann. N. Y. Acad. Sci. 840:317–327.
   PubMedGoogle Scholar
• van Oortmerssen, G. A., and Bakker T. C.. 1981. Artificial selection for short and long attack latencies in wild Mus musculus domesticus. Behav. Genet. 11:115–126.
   PubMed Web of Science ®Google Scholar
• Vartiainen, M. K., Mustonen T., Mattila P. K., Ojala P. J., Thesleff I., Partanen J., and Lappalainen P.. 2002. The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Mol. Biol. Cell 13:183–194.
   PubMed Web of Science ®Google Scholar
• Veenema, A. H., Meijer O. C., De Kloet E. R., Koolhaas J. M., and Bohus B. G.. 2003. Differences in basal and stress-induced HPA regulation of wild house mice selected for high and low aggression. Horm. Behav. 43:197–204.
   PubMed Web of Science ®Google Scholar
• Wakui, H., Wright A. P., Gustafsson J., and Zilliacus J.. 1997. Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein. J. Biol. Chem. 272:8153–8156.
   PubMed Web of Science ®Google Scholar
• Wochnik, G. M., Young J. C., Schmidt U., Holsboer F., Hartl F. U., and Rein T.. 2004. Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90. FEBS Lett. 560:35–38.
   PubMedGoogle Scholar
• Yang, L., Guerrero J., Hong H., DeFranco D. B., and Stallcup M. R.. 2000. Interaction of the tau2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, hic-5, which localizes to both focal adhesions and the nuclear matrix. Mol. Biol. Cell 11:2007–2018.
   PubMed Web of Science ®Google Scholar
• Yang-Yen, H. F., Chambard J. C., Sun Y. L., Smeal T., Schmidt T. J., Drouin J., and Karin M.. 1990. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell 62:1205–1215.
   PubMed Web of Science ®Google Scholar