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Volumn 1763, Issue 8, 2006, Pages 805-814

Intracellular localization of RORα is isoform and cell line-dependent

Author keywords

293 HEK cell; Cellular distribution; Cholesterol; HeLa cell; Nuclear receptor; ROR

Indexed keywords

CELL NUCLEUS RECEPTOR; ISOPROTEIN; RETINOID ORPHAN RECEPTOR ALPHA; UNCLASSIFIED DRUG; CELL RECEPTOR; COMPLEMENTARY DNA; ENHANCED GREEN FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; RAR RELATED ORPHAN RECEPTOR A; RAR-RELATED ORPHAN RECEPTOR A; RETINOIC ACID RECEPTOR; TRANSACTIVATOR PROTEIN;

EID: 33747011645     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2006.05.006     Document Type: Article
Times cited : (15)

References (50)
  • 1
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans R.M. The steroid and thyroid hormone receptor superfamily. Science 240 (1988) 889-895
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 2
    • 0026784326 scopus 로고
    • Orphan receptors: in search of a unifying hypothesis for activation
    • O'Malley B.W., and Conneely O.M. Orphan receptors: in search of a unifying hypothesis for activation. Mol. Endocrinol. 6 (1992) 1359-1361
    • (1992) Mol. Endocrinol. , vol.6 , pp. 1359-1361
    • O'Malley, B.W.1    Conneely, O.M.2
  • 3
    • 0030462820 scopus 로고    scopus 로고
    • Orphan nuclear receptors-the first eight years
    • Enmark E., and Gustafsson J.A. Orphan nuclear receptors-the first eight years. Mol. Endocrinol. 10 (1996) 1293-1307
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1293-1307
    • Enmark, E.1    Gustafsson, J.A.2
  • 4
    • 0022453518 scopus 로고
    • Functional domains of the human glucocorticoid receptor
    • Giguere V., Hollenberg S.M., Rosenfeld M.G., and Evans R.M. Functional domains of the human glucocorticoid receptor. Cell 46 (1986) 645-652
    • (1986) Cell , vol.46 , pp. 645-652
    • Giguere, V.1    Hollenberg, S.M.2    Rosenfeld, M.G.3    Evans, R.M.4
  • 5
    • 0022720813 scopus 로고
    • The chicken oestrogen receptor sequence: homology with v-erbA and the human oestrogen and glucocorticoid receptors
    • Krust A., Green S., Argos P., Kumar V., Walter P., Bornert J.M., and Chambon P. The chicken oestrogen receptor sequence: homology with v-erbA and the human oestrogen and glucocorticoid receptors. EMBO J. 5 (1986) 891-897
    • (1986) EMBO J. , vol.5 , pp. 891-897
    • Krust, A.1    Green, S.2    Argos, P.3    Kumar, V.4    Walter, P.5    Bornert, J.M.6    Chambon, P.7
  • 6
    • 0027446362 scopus 로고
    • The orphan nuclear receptor NGFI-B regulates expression of the gene encoding steroid 21-hydroxylase
    • Wilson T.E., Mouw A.R., Weaver C.A., Milbrandt J., and Parker K.L. The orphan nuclear receptor NGFI-B regulates expression of the gene encoding steroid 21-hydroxylase. Mol. Cell. Biol. 13 (1993) 861-868
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 861-868
    • Wilson, T.E.1    Mouw, A.R.2    Weaver, C.A.3    Milbrandt, J.4    Parker, K.L.5
  • 7
    • 0036646515 scopus 로고    scopus 로고
    • Formation of an hER alpha-COUP-TFI complex enhances hER alpha AF-1 through Ser118 phosphorylation by MAPK
    • Metivier R., Gay F.A., Hubner M.R., Flouriot G., Salbert G., Gannon F., Kah O., and Pakdel F. Formation of an hER alpha-COUP-TFI complex enhances hER alpha AF-1 through Ser118 phosphorylation by MAPK. EMBO J. 21 (2002) 3443-3453
    • (2002) EMBO J. , vol.21 , pp. 3443-3453
    • Metivier, R.1    Gay, F.A.2    Hubner, M.R.3    Flouriot, G.4    Salbert, G.5    Gannon, F.6    Kah, O.7    Pakdel, F.8
  • 8
    • 0033120030 scopus 로고    scopus 로고
    • Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1
    • Tremblay A., Tremblay G.B., Labrie F., and Giguere V. Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1. Mol. Cell 3 (1999) 513-519
    • (1999) Mol. Cell , vol.3 , pp. 513-519
    • Tremblay, A.1    Tremblay, G.B.2    Labrie, F.3    Giguere, V.4
  • 9
    • 0034061186 scopus 로고    scopus 로고
    • Nuclear transport and transcription
    • Komeili A., and O'Shea E.K. Nuclear transport and transcription. Curr. Opin. Cell Biol. 12 (2000) 355-360
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 355-360
    • Komeili, A.1    O'Shea, E.K.2
  • 11
    • 0029943273 scopus 로고    scopus 로고
    • Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera
    • 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
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 4845-4850
    • Htun, H.1    Barsony, J.2    Renyi, I.3    Gould, D.L.4    Hager, G.L.5
  • 12
    • 0032539721 scopus 로고    scopus 로고
    • Subcellular localization of mineralocorticoid receptors in living cells: effects of receptor agonists and antagonists
    • Fejes-Toth G., Pearce D., and Naray-Fejes-Toth A. Subcellular localization of mineralocorticoid receptors in living cells: effects of receptor agonists and antagonists. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 2973-2978
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2973-2978
    • Fejes-Toth, G.1    Pearce, D.2    Naray-Fejes-Toth, A.3
  • 13
    • 0024372113 scopus 로고
    • Mechanisms of nuclear localization of the progesterone receptor: evidence for interaction between monomers
    • Guiochon-Mantel A., Loosfelt H., Lescop P., Sar S., Atger M., Perrot-Applanat M., and Milgrom E. Mechanisms of nuclear localization of the progesterone receptor: evidence for interaction between monomers. Cell 57 (1989) 1147-1154
    • (1989) Cell , vol.57 , pp. 1147-1154
    • Guiochon-Mantel, A.1    Loosfelt, H.2    Lescop, P.3    Sar, S.4    Atger, M.5    Perrot-Applanat, M.6    Milgrom, E.7
  • 14
    • 0032941272 scopus 로고    scopus 로고
    • Differential localization and activity of the A- and B-forms of the human progesterone receptor using green fluorescent protein chimeras
    • Lim C.S., Baumann C.T., Htun H., Xian W., Irie M., Smith C.L., and Hager G.L. Differential localization and activity of the A- and B-forms of the human progesterone receptor using green fluorescent protein chimeras. Mol. Endocrinol. 13 (1999) 366-375
    • (1999) Mol. Endocrinol. , vol.13 , pp. 366-375
    • Lim, C.S.1    Baumann, C.T.2    Htun, H.3    Xian, W.4    Irie, M.5    Smith, C.L.6    Hager, G.L.7
  • 15
    • 0023441954 scopus 로고
    • Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor
    • Picard D., and Yamamoto K.R. Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J. 6 (1987) 3333-3340
    • (1987) EMBO J. , vol.6 , pp. 3333-3340
    • Picard, D.1    Yamamoto, K.R.2
  • 16
    • 0030948745 scopus 로고    scopus 로고
    • Trafficking of the androgen receptor in living cells with fused green fluorescent protein-androgen receptor
    • Georget V., Lobaccaro J.M., Terouanne B., Mangeat P., Nicolas J.C., and Sultan C. Trafficking of the androgen receptor in living cells with fused green fluorescent protein-androgen receptor. Mol. Cell. Endocrinol. 129 (1997) 17-26
    • (1997) Mol. Cell. Endocrinol. , vol.129 , pp. 17-26
    • Georget, V.1    Lobaccaro, J.M.2    Terouanne, B.3    Mangeat, P.4    Nicolas, J.C.5    Sultan, C.6
  • 17
    • 0142211276 scopus 로고    scopus 로고
    • Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor
    • Saporita A.J., Zhang Q., Navai N., Dincer Z., Hahn J., Cai X., and Wang Z. Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor. J. Biol. Chem. 278 (2003) 41998-42005
    • (2003) J. Biol. Chem. , vol.278 , pp. 41998-42005
    • Saporita, A.J.1    Zhang, Q.2    Navai, N.3    Dincer, Z.4    Hahn, J.5    Cai, X.6    Wang, Z.7
  • 18
    • 0032538637 scopus 로고    scopus 로고
    • Hormone-induced translocation of thyroid hormone receptors in living cells visualized using a receptor green fluorescent protein chimera
    • Zhu X.G., Hanover J.A., Hager G.L., and Cheng S.Y. Hormone-induced translocation of thyroid hormone receptors in living cells visualized using a receptor green fluorescent protein chimera. J. Biol. Chem. 273 (1998) 27058-27063
    • (1998) J. Biol. Chem. , vol.273 , pp. 27058-27063
    • Zhu, X.G.1    Hanover, J.A.2    Hager, G.L.3    Cheng, S.Y.4
  • 19
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny S., and Dreyfuss G. Transport of proteins and RNAs in and out of the nucleus. Cell 99 (1999) 677-690
    • (1999) Cell , vol.99 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 20
    • 0035856514 scopus 로고    scopus 로고
    • DNA binding domains in diverse nuclear receptors function as nuclear export signals
    • 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
    • (2001) Curr. Biol. , vol.11 , pp. 1749-1758
    • Black, B.E.1    Holaska, J.M.2    Rastinejad, F.3    Paschal, B.M.4
  • 21
    • 0036224142 scopus 로고    scopus 로고
    • The dynamic and elusive membrane estrogen receptor-alpha
    • Watson C.S., Campbell C.H., and Gametchu B. The dynamic and elusive membrane estrogen receptor-alpha. Steroids 67 (2002) 429-437
    • (2002) Steroids , vol.67 , pp. 429-437
    • Watson, C.S.1    Campbell, C.H.2    Gametchu, B.3
  • 22
    • 0036224417 scopus 로고    scopus 로고
    • Cellular functions of plasma membrane estrogen receptors
    • Levin E.R. Cellular functions of plasma membrane estrogen receptors. Steroids 67 (2002) 471-475
    • (2002) Steroids , vol.67 , pp. 471-475
    • Levin, E.R.1
  • 23
  • 24
    • 0035203706 scopus 로고    scopus 로고
    • A run for a membrane vitamin D receptor
    • Marcinkowska E. A run for a membrane vitamin D receptor. Biol. Signals Recept. 10 (2001) 341-349
    • (2001) Biol. Signals Recept. , vol.10 , pp. 341-349
    • Marcinkowska, E.1
  • 25
    • 0033574663 scopus 로고    scopus 로고
    • A unified nomenclature system for the nuclear receptor superfamily
    • A unified nomenclature system for the nuclear receptor superfamily. Cell 97 (1999) 161-163
    • (1999) Cell , vol.97 , pp. 161-163
  • 26
    • 0036246250 scopus 로고    scopus 로고
    • Characterization of the retinoid orphan-related receptor-alpha coactivator binding interface: a structural basis for ligand-independent transcription
    • Harris J.M., Lau P., Chen S.L., and Muscat G.E. Characterization of the retinoid orphan-related receptor-alpha coactivator binding interface: a structural basis for ligand-independent transcription. Mol. Endocrinol. 16 (2002) 998-1012
    • (2002) Mol. Endocrinol. , vol.16 , pp. 998-1012
    • Harris, J.M.1    Lau, P.2    Chen, S.L.3    Muscat, G.E.4
  • 27
    • 1842639533 scopus 로고    scopus 로고
    • Crystal structure of the human RORalpha ligand binding domain in complex with cholesterol sulfate at 2.2 A
    • Kallen J., Schlaeppi J.M., Bitsch F., Delhon I., and Fournier B. Crystal structure of the human RORalpha ligand binding domain in complex with cholesterol sulfate at 2.2 A. J. Biol. Chem. 279 (2004) 14033-14038
    • (2004) J. Biol. Chem. , vol.279 , pp. 14033-14038
    • Kallen, J.1    Schlaeppi, J.M.2    Bitsch, F.3    Delhon, I.4    Fournier, B.5
  • 28
    • 0028197552 scopus 로고
    • Isoform-specific amino-terminal domains dictate DNA-binding properties of ROR alpha, a novel family of orphan hormone nuclear receptors
    • Giguere V., Tini M., Flock G., Ong E., Evans R.M., and Otulakowski G. Isoform-specific amino-terminal domains dictate DNA-binding properties of ROR alpha, a novel family of orphan hormone nuclear receptors. Genes Dev. 8 (1994) 538-553
    • (1994) Genes Dev. , vol.8 , pp. 538-553
    • Giguere, V.1    Tini, M.2    Flock, G.3    Ong, E.4    Evans, R.M.5    Otulakowski, G.6
  • 29
    • 0027320913 scopus 로고
    • Identification of nuclear receptor mRNAs by RT-PCR amplification of conserved zinc-finger motif sequences
    • Becker-Andre M., Andre E., and DeLamarter J.F. Identification of nuclear receptor mRNAs by RT-PCR amplification of conserved zinc-finger motif sequences. Biochem. Biophys. Res. Commun. 194 (1993) 1371-1379
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1371-1379
    • Becker-Andre, M.1    Andre, E.2    DeLamarter, J.F.3
  • 30
    • 0031194108 scopus 로고    scopus 로고
    • The structural integrity of ROR alpha isoforms is mutated in staggerer mice: cerebellar coexpression of ROR alpha1 and ROR alpha4
    • Matysiak-Scholze U., and Nehls M. The structural integrity of ROR alpha isoforms is mutated in staggerer mice: cerebellar coexpression of ROR alpha1 and ROR alpha4. Genomics 43 (1997) 78-84
    • (1997) Genomics , vol.43 , pp. 78-84
    • Matysiak-Scholze, U.1    Nehls, M.2
  • 32
    • 3242753505 scopus 로고    scopus 로고
    • mRNA expression of nuclear receptor RZR/RORalpha, melatonin membrane receptor MT, and hydroxindole-O-methyltransferase in different populations of human immune cells
    • Pozo D., Garcia-Maurino S., Guerrero J.M., and Calvo J.R. mRNA expression of nuclear receptor RZR/RORalpha, melatonin membrane receptor MT, and hydroxindole-O-methyltransferase in different populations of human immune cells. J. Pineal Res. 37 (2004) 48-54
    • (2004) J. Pineal Res. , vol.37 , pp. 48-54
    • Pozo, D.1    Garcia-Maurino, S.2    Guerrero, J.M.3    Calvo, J.R.4
  • 35
    • 0031907862 scopus 로고    scopus 로고
    • Orphan nuclear receptor ROR alpha-deficient mice display the cerebellar defects of staggerer
    • Dussault I., Fawcett D., Matthyssen A., Bader J.A., and Giguere V. Orphan nuclear receptor ROR alpha-deficient mice display the cerebellar defects of staggerer. Mech. Dev. 70 (1998) 147-153
    • (1998) Mech. Dev. , vol.70 , pp. 147-153
    • Dussault, I.1    Fawcett, D.2    Matthyssen, A.3    Bader, J.A.4    Giguere, V.5
  • 36
    • 0001152108 scopus 로고
    • Staggerer, a new mutation in the mouse affecting the cerebellum
    • Sidman R.L., Lane P.W., and Dickie M.M. Staggerer, a new mutation in the mouse affecting the cerebellum. Science 137 (1962) 610-612
    • (1962) Science , vol.137 , pp. 610-612
    • Sidman, R.L.1    Lane, P.W.2    Dickie, M.M.3
  • 38
    • 0034254930 scopus 로고    scopus 로고
    • In vitro and in vivo evidence for orphan nuclear receptor RORalpha function in bone metabolism
    • Meyer T., Kneissel M., Mariani J., and Fournier B. In vitro and in vivo evidence for orphan nuclear receptor RORalpha function in bone metabolism. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9197-9202
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9197-9202
    • Meyer, T.1    Kneissel, M.2    Mariani, J.3    Fournier, B.4
  • 39
    • 0037081868 scopus 로고    scopus 로고
    • Age-related phenotypes in the staggerer mouse expand the RORalpha nuclear receptor's role beyond the cerebellum
    • Jarvis C.I., Staels B., Brugg B., Lemaigre-Dubreuil Y., Tedgui A., and Mariani J. Age-related phenotypes in the staggerer mouse expand the RORalpha nuclear receptor's role beyond the cerebellum. Mol. Cell. Endocrinol. 186 (2002) 1-5
    • (2002) Mol. Cell. Endocrinol. , vol.186 , pp. 1-5
    • Jarvis, C.I.1    Staels, B.2    Brugg, B.3    Lemaigre-Dubreuil, Y.4    Tedgui, A.5    Mariani, J.6
  • 40
    • 20444502998 scopus 로고    scopus 로고
    • The orphan nuclear receptor RORalpha regulates circadian transcription of the mammalian core-clock Bmal1
    • Akashi M., and Takumi T. The orphan nuclear receptor RORalpha regulates circadian transcription of the mammalian core-clock Bmal1. Nat. Struct. Mol. Biol. 12 (2005) 441-448
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 441-448
    • Akashi, M.1    Takumi, T.2
  • 41
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0346732296 scopus 로고    scopus 로고
    • The co-repressor hairless protects RORalpha orphan nuclear receptor from proteasome-mediated degradation
    • Moraitis A.N., and Giguere V. The co-repressor hairless protects RORalpha orphan nuclear receptor from proteasome-mediated degradation. J. Biol. Chem. 278 (2003) 52511-52518
    • (2003) J. Biol. Chem. , vol.278 , pp. 52511-52518
    • Moraitis, A.N.1    Giguere, V.2
  • 45
    • 0036606444 scopus 로고    scopus 로고
    • Retinoic acid receptor-related orphan receptor (ROR) alpha4 is the predominant isoform of the nuclear receptor RORalpha in the liver and is up-regulated by hypoxia in HepG2 human hepatoma cells
    • Chauvet C., Bois-Joyeux B., and Danan J.L. Retinoic acid receptor-related orphan receptor (ROR) alpha4 is the predominant isoform of the nuclear receptor RORalpha in the liver and is up-regulated by hypoxia in HepG2 human hepatoma cells. Biochem. J. 364 (2002) 449-456
    • (2002) Biochem. J. , vol.364 , pp. 449-456
    • Chauvet, C.1    Bois-Joyeux, B.2    Danan, J.L.3
  • 48
    • 0029121296 scopus 로고
    • Nuclear export signals and the fast track to the cytoplasm
    • Gerace L. Nuclear export signals and the fast track to the cytoplasm. Cell 82 (1995) 341-344
    • (1995) Cell , vol.82 , pp. 341-344
    • Gerace, L.1
  • 49
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass C.K., and Rosenfeld M.G. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 14 (2000) 121-141
    • (2000) Genes Dev. , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 50
    • 0031725138 scopus 로고    scopus 로고
    • Mechanisms of progesterone receptor export from nuclei: role of nuclear localization signal, nuclear export signal, and ran guanosine triphosphate
    • Tyagi R.K., Amazit L., Lescop P., Milgrom E., and Guiochon-Mantel A. Mechanisms of progesterone receptor export from nuclei: role of nuclear localization signal, nuclear export signal, and ran guanosine triphosphate. Mol. Endocrinol. 12 (1998) 1684-1695
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1684-1695
    • Tyagi, R.K.1    Amazit, L.2    Lescop, P.3    Milgrom, E.4    Guiochon-Mantel, A.5


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