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Volumn 72, Issue 3, 2009, Pages 154-171

Transcriptional activity of ecdysone receptor isoforms is regulated by modulation of receptor stability and interaction with AB- and C-domains of the heterodimerization partner ultraspiracle

Author keywords

Drosophila; Hormonal regulation; Hormone; Insect; Nuclear receptor; Receptor protein stability

Indexed keywords

CF1 PROTEIN, INSECT; DNA BINDING PROTEIN; DROSOPHILA PROTEIN; ECDYSONE RECEPTOR; ISOPROTEIN; STEROID RECEPTOR; TRANSCRIPTION FACTOR;

EID: 65549156340     PISSN: 07394462     EISSN: 15206327     Source Type: Journal    
DOI: 10.1002/arch.20309     Document Type: Article
Times cited : (9)

References (53)
  • 1
    • 33747816546 scopus 로고    scopus 로고
    • Lives and times of nuclear receptors
    • Alarid ET. 2006. Lives and times of nuclear receptors. Mol Endocrinol 20:1972-1981.
    • (2006) Mol Endocrinol , vol.20 , pp. 1972-1981
    • Alarid, E.T.1
  • 2
    • 62949162760 scopus 로고    scopus 로고
    • DNA affects ligand binding of the ecdysone receptor of Drosophila melanogaster
    • Azoitei A, Spindler-Barth M. 2009. DNA affects ligand binding of the ecdysone receptor of Drosophila melanogaster. Mol Cell Endocrinol 303:91-99.
    • (2009) Mol Cell Endocrinol , vol.303 , pp. 91-99
    • Azoitei, A.1    Spindler-Barth, M.2
  • 3
    • 70350726333 scopus 로고    scopus 로고
    • Functional analysis of ecdysteroid receptor from Drosophila melanogaster in vitro
    • In: Smagghe G, editor, Berlin: Springer
    • Azoitei A, Ruff H, Tremmel Ch, Braun S, Spindler-Barth M. 2009. Functional analysis of ecdysteroid receptor from Drosophila melanogaster in vitro. In: Smagghe G, editor. Ecdysone, structures and functions. Berlin: Springer. p 377-388.
    • (2009) Ecdysone, structures and functions , pp. 377-388
    • Azoitei, A.1    Ruff, H.2    Tremmel, C.3    Braun, S.4    Spindler-Barth, M.5
  • 4
    • 33845611963 scopus 로고    scopus 로고
    • Analysis of transcriptional activity mediated by Drosophila melanogaster ecdysone receptor isoforms in a heterologous cell culture system
    • Beatty J, Fauth T, Callender JL, Spindler-Barth M, Henrich VC. 2006. Analysis of transcriptional activity mediated by Drosophila melanogaster ecdysone receptor isoforms in a heterologous cell culture system. Insect Mol Biol 15:785-795.
    • (2006) Insect Mol Biol , vol.15 , pp. 785-795
    • Beatty, J.1    Fauth, T.2    Callender, J.L.3    Spindler-Barth, M.4    Henrich, V.C.5
  • 5
    • 0031455799 scopus 로고    scopus 로고
    • Drosophila ecdysone receptor mutations reveal functional differences among receptor isoforms
    • Bender M, Imam FB, Talbot WS, Ganetzky B, Hogness DS. 1997. Drosophila ecdysone receptor mutations reveal functional differences among receptor isoforms. Cell 91:777-788.
    • (1997) Cell , vol.91 , pp. 777-788
    • Bender, M.1    Imam, F.B.2    Talbot, W.S.3    Ganetzky, B.4    Hogness, D.S.5
  • 6
    • 34447515364 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the ecdysteroid receptor (EcR) and of ultraspiracle (Usp) from Drosophila melanogaster in mammalian cells: Energy requirement and interaction with exportin
    • Betanska K, Nieva C, Spindler-Barth M, Spindler KD. 2007. Nucleocytoplasmic shuttling of the ecdysteroid receptor (EcR) and of ultraspiracle (Usp) from Drosophila melanogaster in mammalian cells: energy requirement and interaction with exportin. Arch Insect Biochem Physiol 65:134-142.
    • (2007) Arch Insect Biochem Physiol , vol.65 , pp. 134-142
    • Betanska, K.1    Nieva, C.2    Spindler-Barth, M.3    Spindler, K.D.4
  • 9
    • 18244381247 scopus 로고    scopus 로고
    • Isoform-dependent actions of thyroid hormone nuclear receptors: Lessons from knockin, mutant mice
    • Cheng SY. 2005. Isoform-dependent actions of thyroid hormone nuclear receptors: lessons from knockin, mutant mice. Steroids 70:450-454.
    • (2005) Steroids , vol.70 , pp. 450-454
    • Cheng, S.Y.1
  • 10
    • 0037262925 scopus 로고    scopus 로고
    • EcR isoforms in Drosophila: Testing tissue-specific requirements by targeted blockade and rescue
    • Cherbas L, Hu X, Zhimulev I, Belyaeva E, Cherbas P. 2003. EcR isoforms in Drosophila: testing tissue-specific requirements by targeted blockade and rescue. Development 130:271-284.
    • (2003) Development , vol.130 , pp. 271-284
    • Cherbas, L.1    Hu, X.2    Zhimulev, I.3    Belyaeva, E.4    Cherbas, P.5
  • 11
    • 33751000477 scopus 로고    scopus 로고
    • Multiple glucocorticoid receptor isoforms and mechanisms of post-translational modification
    • Duma D, Jewell CM, Cidlowski JA. 2006a. Multiple glucocorticoid receptor isoforms and mechanisms of post-translational modification. J Steroid Biochem Mol Biol 102:11-21.
    • (2006) J Steroid Biochem Mol Biol , vol.102 , pp. 11-21
    • Duma, D.1    Jewell, C.M.2    Cidlowski, J.A.3
  • 12
    • 33745090483 scopus 로고    scopus 로고
    • Glucocorticoid receptor isoforms generate transcription specificity
    • Duma D, Jewell CM, Cidlowski JA. 2006b. Glucocorticoid receptor isoforms generate transcription specificity. Trends Cell Biol 16:301-307.
    • (2006) Trends Cell Biol , vol.16 , pp. 301-307
    • Duma, D.1    Jewell, C.M.2    Cidlowski, J.A.3
  • 15
    • 0141706670 scopus 로고    scopus 로고
    • The AF-1 and AF-2 domains of RAR gamma 2 and RXR alpha cooperate for triggering the transactivation and the degradation of RAR gamma 2/RXR alpha heterodimers
    • Gianní M, Tarrade A, Nigro EA, Garattini E, Rochette-Egly C. 2003. The AF-1 and AF-2 domains of RAR gamma 2 and RXR alpha cooperate for triggering the transactivation and the degradation of RAR gamma 2/RXR alpha heterodimers. J Biol Chem 278:34458-34466.
    • (2003) J Biol Chem , vol.278 , pp. 34458-34466
    • Gianní, M.1    Tarrade, A.2    Nigro, E.A.3    Garattini, E.4    Rochette-Egly, C.5
  • 17
    • 0032428044 scopus 로고    scopus 로고
    • The RXR homolog ultraspiracle is an essential component of the Drosophila ecdysone receptor
    • Hall Bl, Thummel CS. 1998. The RXR homolog ultraspiracle is an essential component of the Drosophila ecdysone receptor. Development 125:4709-4717.
    • (1998) Development , vol.125 , pp. 4709-4717
  • 18
    • 85069936917 scopus 로고    scopus 로고
    • The ecdysteroid receptor
    • In: Gilbert LJ, Iatrou K, editors, Oxford: Elsevier, Pergamon Press
    • Henrich VC. 2005. The ecdysteroid receptor. In: Gilbert LJ, Iatrou K, editors. Comprehensive molecular insect science, Vol. 3. Oxford: Elsevier, Pergamon Press. p 243-282.
    • (2005) Comprehensive molecular insect science , vol.3 , pp. 243-282
    • Henrich, V.C.1
  • 20
    • 0344153323 scopus 로고    scopus 로고
    • Juvenile hormone potentiates ecdysone receptor-dependent transcription in a mammalian cell culture system
    • Henrich VC, Burns E, Yelverton DP, Christensen E, Weinberger C. 2003. Juvenile hormone potentiates ecdysone receptor-dependent transcription in a mammalian cell culture system. Insect Biochem Mol Biol 33:1239-1244.
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 1239-1244
    • Henrich, V.C.1    Burns, E.2    Yelverton, D.P.3    Christensen, E.4    Weinberger, C.5
  • 23
    • 3343024438 scopus 로고    scopus 로고
    • Differential control of MHR3 promoter activity by isoforms of the ecdysone receptor and inhibitory effects of E75A and MHR3
    • Hiruma K, Riddiford LM. 2004. Differential control of MHR3 promoter activity by isoforms of the ecdysone receptor and inhibitory effects of E75A and MHR3. Dev Biol 272:510-521
    • (2004) Dev Biol , vol.272 , pp. 510-521
    • Hiruma, K.1    Riddiford, L.M.2
  • 24
    • 0029060144 scopus 로고
    • Ligand-independent and -dependent functions of thyroid hormone receptor isoforms depend upon their distinct amino termini
    • Hollenberg AN, Monden T, Wondisford FE. 1995. Ligand-independent and -dependent functions of thyroid hormone receptor isoforms depend upon their distinct amino termini. J Biol Chem 270:14274-14280.
    • (1995) J Biol Chem , vol.270 , pp. 14274-14280
    • Hollenberg, A.N.1    Monden, T.2    Wondisford, F.E.3
  • 25
    • 0037385168 scopus 로고    scopus 로고
    • Transcription activation by the ecdysone receptor (EcR/USP): Identification of activation functions
    • Hu X, Cherbas L, Cherbas P. 2003. Transcription activation by the ecdysone receptor (EcR/USP): identification of activation functions. Mol Endocrinol 17:716-731.
    • (2003) Mol Endocrinol , vol.17 , pp. 716-731
    • Hu, X.1    Cherbas, L.2    Cherbas, P.3
  • 26
    • 0037245786 scopus 로고    scopus 로고
    • Transactivation functions of the N-terminal domains of nuclear hormone receptors: Protein folding and coactivator interactions
    • Kumar R, Thompson EB. 2003. Transactivation functions of the N-terminal domains of nuclear hormone receptors: protein folding and coactivator interactions. Mol Endocrinol 17:1-10.
    • (2003) Mol Endocrinol , vol.17 , pp. 1-10
    • Kumar, R.1    Thompson, E.B.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 27744511919 scopus 로고    scopus 로고
    • Structure and function of steroid receptor AF1 transactivation domains: Induction of active conformations
    • Lavery DN, McEwan IJ. 2005. Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations. Biochem J 391:449-464.
    • (2005) Biochem J , vol.391 , pp. 449-464
    • Lavery, D.N.1    McEwan, I.J.2
  • 29
    • 0033944751 scopus 로고    scopus 로고
    • A conditional rescue system reveals essential functions for the ecdysone receptor (EcR) gene during molting and metamorphosis in Drosophila
    • Li T, Bender M. 2000. A conditional rescue system reveals essential functions for the ecdysone receptor (EcR) gene during molting and metamorphosis in Drosophila. Development 127:2897-2905.
    • (2000) Development , vol.127 , pp. 2897-2905
    • Li, T.1    Bender, M.2
  • 30
    • 34548252291 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Judges, juries, and executioners of cellular regulation
    • Lonard DM, O'Malley BW. 2007 Nuclear receptor coregulators: judges, juries, and executioners of cellular regulation. Mol Cell 27:691-700.
    • (2007) Mol Cell , vol.27 , pp. 691-700
    • Lonard, D.M.1    O'malley, B.W.2
  • 31
    • 0034825664 scopus 로고    scopus 로고
    • Differential control of gene activity by isoforms A, B1 and B2 of the Drosophila ecdysone receptor
    • Mouillet JF, Henrich VC, Lezzi M, Vögtli M. 2001. Differential control of gene activity by isoforms A, B1 and B2 of the Drosophila ecdysone receptor. Eur J Biochem 268:1811-1819.
    • (2001) Eur J Biochem , vol.268 , pp. 1811-1819
    • Mouillet, J.F.1    Henrich, V.C.2    Lezzi, M.3    Vögtli, M.4
  • 32
    • 0027154780 scopus 로고
    • RARs and RXRs: Evidence for two autonomous transactivation functions (AF-1 and AF-2) and heterodimerization in vivo
    • Nagpal S, Friant S, Nakshatri H, Chambon P. 1993. RARs and RXRs: evidence for two autonomous transactivation functions (AF-1 and AF-2) and heterodimerization in vivo. EMBO J 12:2349-2360.
    • (1993) EMBO J , vol.12 , pp. 2349-2360
    • Nagpal, S.1    Friant, S.2    Nakshatri, H.3    Chambon, P.4
  • 33
    • 0033956886 scopus 로고    scopus 로고
    • Polarity of the ecdysone receptor complex interaction with the palindromic response element from the hsp27 genepromoter
    • Niedziela-Majka A, Kochman M, Ozyhar A. 2000. Polarity of the ecdysone receptor complex interaction with the palindromic response element from the hsp27 genepromoter. Eur J Biochem 267:507-519.
    • (2000) Eur J Biochem , vol.267 , pp. 507-519
    • Niedziela-Majka, A.1    Kochman, M.2    Ozyhar, A.3
  • 35
    • 34948902277 scopus 로고    scopus 로고
    • Influence of hormone on intracellular localization of the Drosophila melanogaster ecdysteroid receptor (EcR)
    • Nieva C, Spindler-Barth M, Azoitei A, Spindler KD. 2007. Influence of hormone on intracellular localization of the Drosophila melanogaster ecdysteroid receptor (EcR). Cell Signal 19: 2582-2587.
    • (2007) Cell Signal , vol.19 , pp. 2582-2587
    • Nieva, C.1    Spindler-Barth, M.2    Azoitei, A.3    Spindler, K.D.4
  • 36
    • 45549083770 scopus 로고    scopus 로고
    • Impact of heterodimerization on intracellular localization of the ecdysteroid receptor (EcR)
    • Nieva C, Spindler-Barth M, Spindler K-D. 2008. Impact of heterodimerization on intracellular localization of the ecdysteroid receptor (EcR). Arch Insect Biochem Physiol 68:40-49.
    • (2008) Arch Insect Biochem Physiol , vol.68 , pp. 40-49
    • Nieva, C.1    Spindler-Barth, M.2    Spindler, K.-D.3
  • 40
    • 84873782420 scopus 로고
    • Genetics of somatic mammalian cells. III. Long-term cultivation of euploid cells from human and animal subjects
    • Puck TT, Cieciura SJ, Robinson A. 1958. Genetics of somatic mammalian cells. III. Long-term cultivation of euploid cells from human and animal subjects. J Exp Med 108:945-956.
    • (1958) J Exp Med , vol.108 , pp. 945-956
    • Puck, T.T.1    Cieciura, S.J.2    Robinson, A.3
  • 41
    • 0001606007 scopus 로고
    • An ecdysone response element in the Drosophila hsp27 promoter
    • Riddihough G, Pelham HR. 1987. An ecdysone response element in the Drosophila hsp27 promoter. EMBO J 6:3729-3734.
    • (1987) EMBO J , vol.6 , pp. 3729-3734
    • Riddihough, G.1    Pelham, H.R.2
  • 42
    • 0027486314 scopus 로고
    • Programmed cell death in the Drosophila CNS is ecdysone-regulated and coupled with a specific ecdysone receptor isoform
    • Robinow S, Talbot WS, Hogness DS, Truman JW. 1993. Programmed cell death in the Drosophila CNS is ecdysone-regulated and coupled with a specific ecdysone receptor isoform. Development 119:1251-1259.
    • (1993) Development , vol.119 , pp. 1251-1259
    • Robinow, S.1    Talbot, W.S.2    Hogness, D.S.3    Truman, J.W.4
  • 43
    • 0042427425 scopus 로고    scopus 로고
    • The N-terminal of the estrogen receptor (ERalpha) mediates transcriptional cross-talk with the retinoic acid receptor in human breast cancer cells
    • Rousseau C, Pettersson F, Couture MC, Paquin A, Galipeau J, Mader S, Miller Jr WH. 2003. The N-terminal of the estrogen receptor (ERalpha) mediates transcriptional cross-talk with the retinoic acid receptor in human breast cancer cells. J Steroid Biochem Mol Biol 86:1-14.
    • (2003) J Steroid Biochem Mol Biol , vol.86 , pp. 1-14
    • Rousseau, C.1    Pettersson, F.2    Couture, M.C.3    Paquin, A.4    Galipeau, J.5    Mader, S.6    Miller Jr, W.H.7
  • 44
    • 0041829102 scopus 로고    scopus 로고
    • Isoform specific control of gene activity in vivo by the Drosophila ecdysone receptor
    • Schubiger M, Tomita S, Sung C, Robinow S, Truman JW. 2003. Isoform specific control of gene activity in vivo by the Drosophila ecdysone receptor. Mech Dev 120:909-918.
    • (2003) Mech Dev , vol.120 , pp. 909-918
    • Schubiger, M.1    Tomita, S.2    Sung, C.3    Robinow, S.4    Truman, J.W.5
  • 46
    • 0027180571 scopus 로고
    • Drosophila tissues with different metamorphic responses to ecdysone express different ecdysone receptor isoforms
    • Talbot WS, Swyryd EA, Hogness DS. 1993. Drosophila tissues with different metamorphic responses to ecdysone express different ecdysone receptor isoforms. Cell 73:1323-1333.
    • (1993) Cell , vol.73 , pp. 1323-1333
    • Talbot, W.S.1    Swyryd, E.A.2    Hogness, D.S.3
  • 47
    • 33747863336 scopus 로고    scopus 로고
    • The N-Terminal A/B domain of the thyroid hormone receptor-beta2 isoform influences ligand-dependent recruitment of coactivators to the ligand-binding domain
    • Tian H, Mahajan MA, Wong CT, Habeos I, Samuels HH. 2006. The N-Terminal A/B domain of the thyroid hormone receptor-beta2 isoform influences ligand-dependent recruitment of coactivators to the ligand-binding domain. Mol Endocrinol 20:2036-2051.
    • (2006) Mol Endocrinol , vol.20 , pp. 2036-2051
    • Tian, H.1    Mahajan, M.A.2    Wong, C.T.3    Habeos, I.4    Samuels, H.H.5
  • 49
    • 0034790342 scopus 로고    scopus 로고
    • Requirement of co- factors for the ligand-mediated activity of the insect ecdysteroid receptor in yeast
    • Tran HAT, Shaaban S, Askari HB, Walfish PG, Raikhek AS, Butt TR. 2001b. Requirement of co- factors for the ligand-mediated activity of the insect ecdysteroid receptor in yeast. J Mol Endocrinol 27:191-209.
    • (2001) J Mol Endocrinol , vol.27 , pp. 191-209
    • Tran, H.A.T.1    Shaaban, S.2    Askari, H.B.3    Walfish, P.G.4    Raikhek, A.S.5    Butt, T.R.6
  • 50
    • 0027955037 scopus 로고
    • Ecdysone receptor expression in the CNS correlates with stage-specific responses to ecdysteroids during Drosophila and Manduca development
    • Truman JW, Talbot WS, Fairbach SE, Hogness DS. 1994. Ecdysone receptor expression in the CNS correlates with stage-specific responses to ecdysteroids during Drosophila and Manduca development. Development 120:219-234.
    • (1994) Development , vol.120 , pp. 219-234
    • Truman, J.W.1    Talbot, W.S.2    Fairbach, S.E.3    Hogness, D.S.4
  • 51
    • 0033180592 scopus 로고    scopus 로고
    • SMRTER, a Drosophila nuclear receptor coregulator, reveals that EcR-mediated repression is critical for development
    • Tsai CC, Kao HY, Yao TP, McKeown M, Evans RM. 1999. SMRTER, a Drosophila nuclear receptor coregulator, reveals that EcR-mediated repression is critical for development. Mol Cell 4:175-186.
    • (1999) Mol Cell , vol.4 , pp. 175-186
    • Tsai, C.C.1    Kao, H.Y.2    Yao, T.P.3    McKeown, M.4    Evans, R.M.5
  • 52
    • 22344452245 scopus 로고    scopus 로고
    • Corepressor binding to progesterone and glucocorticoid receptors involves the activation function-1 domain and is inhibited by molybdate
    • Wang D, Simons Jr SS. 2005. Corepressor binding to progesterone and glucocorticoid receptors involves the activation function-1 domain and is inhibited by molybdate. Mol Endocrinol 19:1483-1500.
    • (2005) Mol Endocrinol , vol.19 , pp. 1483-1500
    • Wang, D.1    Simons Jr, S.S.2
  • 53
    • 0028809317 scopus 로고
    • Specificity of ligand- dependent androgen receptor stabilization: Receptor domain interactions influence ligand dissociation and receptor stability
    • Zhou ZX, Lane MV, Kemppainen JA, French FS, Wilson EM. 1995. Specificity of ligand- dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability. Mol Endocrinol 9:208-218.
    • (1995) Mol Endocrinol , vol.9 , pp. 208-218
    • Zhou, Z.X.1    Lane, M.V.2    Kemppainen, J.A.3    French, F.S.4    Wilson, E.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.