The variety of complexes formed by EcR and Usp nuclear receptors in the nuclei of living cells

Molecular and Cellular Endocrinology

Volumn 294, Issue 1-2, 2008, Pages 45-51

  Dutko Gwóźdź, Joanna ^a   Gwóźdź, Tomasz ^a   Orłowski, Marek ^a   Greb Markiewicz, Beata ^a   Duś, Danuta ^b   Dobrucki, Jurek ^c   Ozyhar, Andrzej ^a  

^a WROCLAW UNIVERSITY OF TECHNOLOGY   (Poland)

^b INSTITUTE OF IMMUNOLOGY AND EXPERIMENTAL THERAPY   (Poland)

^c JAGIELLONIAN UNIVERSITY   (Poland)

Author keywords

20 Hydroxyecdysone; Bimolecular fluorescence complementation; Ecdysteroid receptor; Ultraspiracle

Indexed keywords

CELL NUCLEUS RECEPTOR; ECDYSONE RECEPTOR; ECDYSTEROID; ULTRASPIRACLE RECEPTOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL NUCLEUS; CELL STRAIN COS7; CELLULAR DISTRIBUTION; CHO CELL; COMPLEX FORMATION; CONTROLLED STUDY; DIMERIZATION; FLOW CYTOMETRY; FLUORESCENCE; GENE SWITCHING; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN INDUCTION; PROTEIN PROTEIN INTERACTION;

EID: 53649087510     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2008.07.021     Document Type: Article

References (36)

1. Black B.E., Holaska J.M., Rastinejad F., and Paschal B.M. DNA binding domains in diverse nuclear receptors function as nuclear export signals. Curr. Biol. 11 (2001) 1749-1758
2. Bunn C.F., Neidig J.A., Freidinger K.E., Stankiewicz T.A., Weaver B.S., McGrew J., and Allison L.A. Nucleocytoplasmic shuttling of the thyroid hormone receptor alpha. Mol. Endocrinol. 15 (2001) 512-533
3. Christopherson K.S., Mark M.R., Bajaj V., and Godowski P.J. Ecdysteroid-dependent regulation of genes in mammalian cells by a Drosophila ecdysone receptor and chimeric transactivators. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 6314-6318
4. Dobens L., Rudolph K., and Berger E.M. Ecdysterone regulatory elements function as both transcriptional activators and repressors. Mol. Cell. Biol. 11 (1991) 1846-1853
5. Elmogy M., Iwami M., and Sakurai S. Presence of membrane ecdysone receptor in the anterior silk gland of the silkworm Bombyx mori. Eur. J. Biochem. 271 (2004) 3171-3179
6. Escriva H., Bertrand S., and Laudet V. The evolution of the nuclear receptor superfamily. Essays Biochem. 40 (2004) 11-26
7. Fang F., Xu Y., Jones D., and Jones G. Interactions of ultraspiracle with ecdysone receptor in the transduction of ecdysone- and juvenile hormone-signaling. FEBS J. 272 (2005) 1577-1589
8. Grebe M., Fauth T., and Spindler-Barth M. Dynamic of ligand binding to Drosophila melanogaster ecdysteroid receptor. Insect. Biochem. Mol. Biol. 34 (2004) 981-989
9. Grinberg A.V., Hu C.D., and Kerppola T.K. Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells. Mol. Cell. Biol. 24 (2004) 4294-4308
10. Gwozdz T., Dutko-Gwozdz J., Nieva C., Betanska K., Orlowski M., Kowalska A., Dobrucki J., Spindler-Barth M., Spindler K.D., and Ozyhar A. EcR and Usp, components of the ecdysteroid nuclear receptor complex, exhibit differential distribution of molecular determinants directing subcellular trafficking. Cell. Signal. 19 (2007) 490-503
11. Hager G.L., Lim C.S., Elbi C., and Baumann C.T. Trafficking of nuclear receptors in living cells. J. Steroid Biochem. Mol. Biol. 74 (2000) 249-254
12. Hager G.L., Smith C.L., Fragoso G., Wolford R., Walker D., Barsony J., and Htun H. Intranuclear trafficking and gene targeting by members of the steroid/nuclear receptor superfamily. J. Steroid. Biochem. Mol. Biol. 65 (1998) 125-132
13. Htun H., Barsony J., Renyi I., Gould D.L., and Hager G.L. Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 4845-4850
14. Hu C.D., Chinenov Y., and Kerppola T.K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9 (2002) 789-798
15. Hu X., Cherbas L., and Cherbas P. Transcription activation by the ecdysone receptor (EcR/USP): identification of activation functions. Mol. Endocrinol. 17 (2003) 716-731
16. Karns L.R., Kisielewski A., Gulding K.M., Seraj J.M., and Theodorescu D. Manipulation of gene expression by an ecdysone-inducible gene switch in tumor xenografts. BMC Biotechnol. 1 (2001) 11
17. Katagiri Y., Takeda K., Yu Z.X., Ferrans V.J., Ozato K., and Guroff G. Modulation of retinoid signalling through NGF-induced nuclear export of NGFI-B. Nat. Cell Biol. 2 (2000) 435-440
18. Kerppola T.K. Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell. Biol. 7 (2006) 449-456
19. King-Jones K., and Thummel C.S. Nuclear receptors-a perspective from Drosophila. Nat. Rev. Genet. 6 (2005) 311-323
20. Koelle M.R., Talbot W.S., Segraves W.A., Bender M.T., Cherbas P., and Hogness D.S. The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily. Cell 67 (1991) 59-77
21. Lafont R., and Dinan L. Practical uses for ecdysteroids in mammals including humans: an update. J. Insect. Sci. 3 (2003) 7
22. Laudet V., and Gronemeyer H. The Nuclear Receptor: Factbook (2002), Academic Press, San Diego
23. Nieva C., Gwozdz T., Dutko-Gwozdz J., Wiedenmann J., Spindler-Barth M., Wieczorek E., Dobrucki J., Dus D., Henrich V., Ozyhar A., and Spindler K.D. Ultraspiracle promotes the nuclear localization of ecdysteroid receptor in mammalian cells. Biol. Chem. 386 (2005) 463-470
24. No D., Yao T.P., and Evans R.M. Ecdysone-inducible gene expression in mammalian cells and transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 3346-3351
25. Oro A.E., McKeown M., and Evans R.M. Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor. Nature 347 (1990) 298-301
26. Palli S.R., Hormann R.E., Schlattner U., and Lezzi M. Ecdysteroid receptors and their applications in agriculture and medicine. Vitam. Horm. 73 (2005) 59-100
27. Piehler J. New methodologies for measuring protein interactions in vivo and in vitro. Curr. Opin. Struct. Biol. 15 (2005) 4-14
28. Prufer K., and Barsony J. Retinoid X receptor dominates the nuclear import and export of the unliganded vitamin D receptor. Mol. Endocrinol. 16 (2002) 1738-1751
29. Reits E.A., and Neefjes J.J. From fixed to FRAP: measuring protein mobility and activity in living cells. Nat. Cell. Biol. 3 (2001) E145-E147
30. Riddiford L.M., Cherbas P., and Truman J.W. Ecdysone receptors and their biological actions. Vitam. Horm. 60 (2000) 1-73
31. Rymarczyk G., Grad I., Rusek A., Oswiecimska-Rusin K., Niedziela-Majka A., Kochman M., and Ozyhar A. Purification of Drosophila melanogaster ultraspiracle protein and analysis of its A/B region-dependent dimerization behavior in vitro. Biol. Chem. 384 (2003) 59-69
32. Schlattner U., Vafopoulou X., Steel C.G., Hormann R.E., and Lezzi M. Non-genomic ecdysone effects and the invertebrate nuclear steroid hormone receptor EcR-new role for an "old" receptor?. Mol. Cell. Endocrinol. 247 (2006) 64-72
33. Shank L.C., and Paschal B.M. Nuclear transport of steroid hormone receptors. Crit. Rev. Eukaryot. Gene Expr. 15 (2005) 49-73
34. Tyagi R.K., Lavrovsky Y., Ahn S.C., Song C.S., Chatterjee B., and Roy A.K. Dynamics of intracellular movement and nucleocytoplasmic recycling of the ligand-activated androgen receptor in living cells. Mol. Endocrinol. 14 (2000) 1162-1174
35. Yan Y., and Marriott G. Fluorescence resonance energy transfer imaging microscopy and fluorescence polarization imaging microscopy. Methods Enzymol. 360 (2003) 561-580
36. Yao T.P., Forman B.M., Jiang Z., Cherbas L., Chen J.D., McKeown M., Cherbas P., and Evans R.M. Functional ecdysone receptor is the product of EcR and Ultraspiracle genes. Nature 366 (1993) 476-479