Abstract
There is a wealth of information regarding the import and export of nuclear proteins in general. Nevertheless, the available data that deals with the nucleocytoplasmic movement of steroid hormone receptors remains highly limited. Some research findings reported during the past five years have succeeded in identifying proteins related to the movement of estrogen receptor α from the cytoplasm to the nucleus. What is striking in these findings is the facilitatory role of estradiol in the transport process. A similar conclusion has been drawn from the studies on the plasma membrane-to nucleus movement of the alternative form of estrogen receptor, the non-activated estrogen receptor (naER). The internalization of naER from the plasma membrane takes place only in the presence of estradiol. While the gene regulatory functions of ERα appear to get terminated following its ubiquitinization within the nucleus, the naER, through its deglycosylated form, the nuclear estrogen receptor II (nER II) continues to remain functional even beyond its existence within the nucleus. Recent studies have indicated the possibility that the estrogen receptor that regulates the nucleo cytoplasmic transport of m RNP is the nERII. This appears to be the result of the interaction between nERII and three proteins belonging to a group of small nuclear ribonucleo proteins (snRNP). The interaction of nERII with two of this protein appears to activate the inherent Mg2+ ATPase activity of the complex, which leads to the exit of the RNP through the nuclear pore complex.
Similar content being viewed by others
References
Maul GG: The nuclear and the cytoplasmic pore complex: Structure, dynamics, distribution, and evolution. Int Rev Cytol 6(suppl): 75-186, 1977
Rout MP, Blobel G: Isolation of the yeast nuclear pore complex. J Cell Biol 123: 771-783, 1993
Mattaj IW, Englmeier L: Nucleocytoplasmic transport: The soluble phase. Annu Rev Biochem 67: 265-306, 1998
Macara IG: Transport into and out of the nucleus. Microbiol Mol Biol Rev 65: 570-594, 2001
Stewart M, Baker RP, Bayliss R, Clayton L, Grant RP, Littlewood T, Matsuura Y: Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import. FEBS Lett 498: 145-149, 2001
Ribbeck K, Gorlich D: Kinetic analysis of translocation through nuclear pore complexes. EMBO J 20: 1320-1330, 2001
Pinol-Roma S, Dreyfuss G: Shuttling of pre-MRNA binding proteins between nucleus and cytoplasm. Nature 355: 730-732, 1992
Thampan TNRV, Clark JH: An estrogen receptor activator protein in rat uterine cytosol. Nature 290: 152-154, 1981
Thampan RV: A 62 kDa protein functions as estrogen receptor activation factor (E-RAF) in the goat uterus. Mol Cell Endocrinol 53: 119-130, 1987
Thampan RV: Molecular aspects of estrogen receptor activation factor function. Mol Cell Endocrinol 64: 19-34, 1989
Govind AP, Sreeja S, Thampan RV: (a) Proteins that mediate the nuclear entry of the goat uterine estrogen receptor activation factor (E-RAF): Identification of a molecular basis for the inhibitory effect of progesterone on estrogen action. J Cell Biochem (in press)
Govind AP, Sreeja S, Thampan RV: (b) Estradiol dependent anchoring of the goat uterine estrogen receptor activation factor (E-RAF) at the endoplasmic reticulum by a 55 kDa anchor protein (ap 55). J Cell Biochem (in press)
Sreeja S: Molecular mechanisms associated with the plasma membrane-to-nucleus movement of the goat uterine non-activated estrogen receptor. Ph.D. Thesis, University of Kerala, 2001
Kalderon D, Roberts BL, Richardson WD, Smith AE: A short amino acid sequence able to specify nuclear location. Cell 39: 499-509, 1984
Robbins J, Dilworth SM, Laskey RA, Dingwall C: Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence. Cell 64: 615-623, 1991
Imamoto N, Tachibana T, Matsubae M, Yoneda Y: A karyophilic protein forms a stable complex with cytoplasmic component prior to nuclear pore binding. J Biol Chem 270: 8559-8565, 1995
Gorlich D, Kostka S, Kraft R, Dingwall C, Laskey RA, Hartmann E, Prehn S: Two different subunits of importin cooperates to recognize nuclear localization signal and bind them to the nuclear envelope. Curr Biol 5: 383-392, 1995
Moroianu J, Blobel G, Radu A: Previously identified protein of uncertain function is karyopherin α and together with karyopherin β docks import substrate at nuclear pore complex. Proc Natl Acad Sci USA 92: 2008-2011, 1995
Moore MS, Blobel G: The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature 365: 661-663, 1993
Moore MS, Blobel G: Purification of Ran-interacting protein that is required for protein import into the nucleus. Proc Natl Acad Sci USA 10: 10212-10216, 1994
Paschal BM, Gerace L: Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62. J Cell Biol 129: 925-937, 1995
Doye V, Hurt E: From nucleoporins to nuclear pore complexes. Curr Opin Cell Biol 9: 401-411, 1997
Yoshida K, Blobel G: The karyopherin Kap 142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins. J Cell Biol 152: 729-740, 2001
Mingot J.-M, Kostka S, Kraft R, Hartmann E, Gorlich D: Importin 13: A novel mediator of nuclear import and export. EMBO J 20: 3685-3694, 2001
Siomi H, Dreyfuss G: A nuclear localization domain in the hnRNPA1 protein. J Cell Biol 129: 551-560, 1995
Pollard VW, Michael WM, Nakielny S, Siomi MC, Wang F, Dreyfuss G: A novel receptor-mediated nuclear protein import pathway. Cell 86: 985-994, 1996
Aitchison JD, Blobel G, Rout MP: Kap104p: A karyopherin involved in the nuclear transport of messenger RNA binding proteins. Science 274: 624-627, 1996
Luhrmann R, Kastner B, Bach M: Structure of spliceosomal snRNPs and their role in pre-mRNA splicing. Biochim Biophys Acta 1087: 265-292, 1990
Fischer U, Luhrmann R: An essential signaling role for the m3G-cap in the transport of U1 snRNP to the nucleus. Science 249: 786-790, 1990
Huber J, Cronshagen U, Kadokura M, Marshallsay C, Wada T, Sekine M, Luhrmann R: Snurportin 1, an m3G-cap-specific nuclear import receptor with a novel domain structure. EMBO J 17: 4114-4126, 1998
Schaap PJ, van't Riet J, Woldringh CL, Raue HA: Identification and functional analysis of the nuclear localization signals of ribosomal protein L25 from Saccharomyces cerevisiae. J Mol Biol 221: 225-237, 1991
Kambach C, Mattaj IW: Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA. J Cell Biol 118: 11-21, 1992
Izaurralde E, Jarmolowski A, Beisel C, Mattaj IW, Dreyfuss G, Fischer U: A role for the M9 transport signal of hnRNP A1 in mRNA nuclear export. J Cell Biol 137: 27-35, 1997
Bischoff FR, Klebe C, Kretschmer J, Wittingghofer A, Ponstingl H: RanGAP1 induces GTPase activity of nuclear ras-related Ran. Proc Natl Acad Sci USA 91: 2587-2591, 1994
Bischoff FR, Ponstingl H: Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC I. Nature 354: 80-82, 1991
Weis K: Nucleocytoplasmic transport: Cargo trafficking across the border. Curr Opin Cell Biol 14: 328-335, 2002
Gorlich D, Pante N, Kutay U, Aebi U, Bischoff FR: Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J 15: 5584-5594, 1996
Guiochon-Mantel A, Lescop P, Christin-Maitre S, Loosefelt H, Perrot Appalant M, Milgrom E: Nucleocytoplasmic shuttling of the progesterone receptor. EMBO J 10: 3851-3859, 1991
Dauvois S, White R, Parker MG: The anti estrogen ICI 182780 disrupts estrogen receptor nuclcocytoplasmic shuttling. J Cell Sci 106: 1377-1388, 1993
Madan AP, DeFranco DB: Bidirectional transport of glucocorticoid receptors across the nuclear envelope. Proc Natl Acad Sci USA 90: 3588-3592, 1993
LaCasse EC, Lefebvre YA: Nuclear localization signals overlap DNA or RNA-binding domains in nucleic acid-binding proteins. Nucleic Acids Res 23: 1647-1656, 1995
Guiochon-Mantel A, Lescop P, Sar S, Atger M, Perrot Applanant M, Milgrom E: Mechanisms of nuclear localization of the progesterone receptor: Evidence for interactions between monomers. Cell 57: 1147-1154, 1989
Ylikomi T, Bocquel MT, Berry M, Gronemeyer H, Chambon P: Cooperation of proto-signals for nuclear accumulation of estrogen and progesterone receptors. EMBO J 11: 3681-3694, 1992
Picard D, Yamamoto KR: Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J 6: 3333-3340, 1987
Picard D, Kumar V, Chambon P, Yamamoto KR: Signal transduction by steroid hormones: Nuclear localization is differentiately regulated in estrogen and progesterone receptors. Cell Regul 1: 291-299, 1990b
Picard D, Khursheed B, Garabedian MJ, Fortin MG, Lindquist S, Yamamoto KR: Reduced levels of hsp90 compromise steroid action in vivo. Nature 348: 166-168, 1990a
Sai Padma A, Renil M, Thampan RV: Protein-protein interactions that precede the nuclear entry of goat uterine estrogen receptor under cell-free conditions. J Cell Biochem 78: 650-665, 2000b
Welshons W, Lieberman ME, Gorski J: Nuclear localization of unoccupied estrogen receptors: Cytochalasin nucleation of GH3 cells. Nature 307: 747-749, 1984
Sackey FNA, Hache RJG, Reich T, Kwast-Welfeld J, Lefebvre YA: Determinants of subcellular distribution of the glucocorticoid receptor. Mol Endocrinol 10: 1191-1205, 1996
Pratt WB, Toft DO: Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18: 306-60, 1997
Bresnick EH, Dalman FC, Sanchez ER, Pratt WB: Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J Biol Chem 264: 4992-4997, 1989
Cadepond F, Schweizergroyer G, Segardmaurel L, Jibard N, Holenberg SM, Giguere V, Evans RM, Baulieu EE: Heat shock protein-90 as a critical factor in maintaining glucocortocosteroid receptor in a nonfunctional state. J Biol Chem 266: 5834-5841, 1991
Qi M, Hamilton BJ, DeFranco DB: V-mos oncoproteins affect the nuclear retention and reutilization of glucocorticoid receptors. Mol Endocrinol 3: 1279-1288, 1989
Beg AA, Ruben SM, Scheinman RI, Haskill S, Rosen CA, Baldwin Jr AS: I kappa B interacts with the nuclear localization sequences of the subunits of NF-Kappa B: A mechanism for cytoplasmic retention. Genes Dev 6: 1899-1913, 1992
Ganchi PA, Sun SC, Greene WC, Ballard DW: I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B65 DNA binding. Mol Biol Cell 3: 1339-1352, 1992
Puca GA, Medici N, Armetta I, Nigro V, Moncharmont B, Molinari AM: Interaction between estrogen receptor and subcellular structures of target cells: Nuclear localization of unoccupied receptor and its modification induced by estradiol. Ann NY Acad Sci 464: 168-189, 1986
Press MF, Greene GL: Localization of progesterone receptor with monoclonal antibodies to the human progesterone receptor. Endocrinology 122: 1165-1175, 1988
Yang J, Liu J, DeFranco DB: Subnuclear trafficking of glucocorticoid receptors in vitro: Chromatin recycling and nuclear export. J Cell Biol 137: 523-538, 1997
Sanchez ER, Hirst M, Scherrer LC, Tang HY, Welsh MJ, Harmon JM, Simons SSJ, Ringold GM, Pratt WB: Hormone free mouse glucocorticoid receptors over expressed in Chinese hamster ovary cells are localized to the nucleus and are associated with both hsp 70 and hsp90. J Biol Chem 265: 20123-20130, 1990
Martins VR, Pratt WB, Terracio L, Hirst MA, Ringold GM, Housley PR: Demonstration by confocal microscopy that unliganded over expressed glucocorticoid receptors are distributed in a non random manner throughout all planes of the nucleus. Mol Endocrinol 5: 217-225, 1991
Jewell CM, Webster JC, Burnstein KL, Sar M, Bodwell JE, Cidlowski JA: Immunocytochemical analysis of hormone mediated nuclear trans-location of wild type and mutant glucocorticoid receptors. J Steroid Biochem Mol Biol 55: 135-146, 1995
Nirmala PB, Thampan RV: A 55 kDa protein (p55) of the goat uterus mediates nuclear transport of the estrogen receptor. I. Purification and characterization. Arch Biochem Biophys 319: 551-561, 1995a
Nirmala PB, Thampan RV: A 55 kDa protein (p55) of the goat uterus mediates nuclear transport of the estrogen receptor. II. Details of the transport mechanism. Arch Biochem Biophys 319: 562-569, 1995b
Sai Padma A, Thampan RV: Interdependence between a 55 kDa Protein (p55) and a 12 kDa Protein (p12) in facilitating the nuclear entry of goat uterine estrogen receptor under cell-free conditions. Biol Chem 381: 285-294, 2000a
Izaurralde E, Adam S: Transport of macromolecules between the nucleus and the cytoplasm. RNA 4: 351-364, 1998
Klemm JD, Beals CR, Crabtree GR: Rapid targeting of nuclear proteins to the cytoplasm. Curr Biol 7: 638-644, 1997
Fischer U, Huber J, Boelens WC, Mattaj IW, Luhrmann R: The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82: 475-483, 1995
Richards SA, Lounsbury KM, Carey KL, Macara IG: A nuclear export signal is essential for the cytoplasmic localization of the Ran binding protein, RanBP1. J Cell Biol 134: 1157-1168, 1996
Wen W, Meinkoth JL, Tsien RY, Taylor SS: Identification of a signal for rapid export of proteins from the nucleus. Cell 82: 463-473, 1995
Fornerod M, Ohno M, Yoshida M, Mattaj IW: CRMI is an export receptor for leucine-rich nuclear export signals. Cell 90: 1051-1060, 1997
Adachi Y, Yanagida M: Higher order chromosome structure is affected by cold-sensitive mutations in a Schizo-saccharomyces pombe gene CRM1+, which encodes a 115-kDa protein preferentially localized in the nucleus and its periphery. J Cell Biol 108: 1195-1207, 1989
Kutay U, Bischoff FR, Kostka S, Kraft R, Gorlich D: Export of importin alpha from the nucleus is mediated by specific nuclear transport factor. Cell 90: 1061-1071, 1997
Reed R, Magni K: A new view of mRNA export: Separating the wheat from the chaff. Nat Cell Biol 3: 201-204, 2001
Calado A, Treichel N, Muller EC, Otto A, Kutay U: Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO J 21: 6216-6224, 2002
Michael WM, Choi M, Dreyfuss G: A nuclear export signal in hnRNPA1: A signal-mediated, temperature-dependent nuclear protein export pathway. Cell 83: 415-422, 1995a
Michel WM, Eder PS, Dreyfuss G: The K nuclear shuttling domain: A novel signal for nuclear import and nuclear export in the hnRNP K protein. EMBO J 16: 3587-3598, 1995b
Fan XC, Steitz JA: HNS, a nuclear-cytoplasmic shuttling sequence in HuR. Proc Natl Acad Sci USA 95: 15293-15298, 1998
Holaska JM, Black BE, Love DC, Hanover JA, Leszyk J, Paschal BM: Calreticulin is a receptor for nuclear export. J Cell Biol 152: 127-140, 2001
Wikstrom AC, Bakke O, Okret S, Bronnegard M, Gustafsson JA: Intracellular localization of the glucocorticoid receptor: Evidence for cytoplasmic and nuclear localization. Endocrinology 120: 1232-1242, 1987
Cidlowski JA, Lbellingham D, Powell-Oliver FE, Lubahn DB, Sar M: Novel antipeptide antibodies to the human glucocorticoid receptor: Recognition of multiple distinct receptor forms in vitro and distinct localization of cytoplasmic and nuclear receptors. Mol Endocrinol 4: 1427-1437, 1990
Orti E, Mendel DB, Smith LI, Bodwell JE, Munck A: A dynamic model of glucocorticoid receptor phosphor elation and recycling in intact cells. J Steroid Biochem 34: 85-96, 1989
Chandran UR, DeFranco DB: Internuclear migration of chicken progesterone receptor, but not semia virus-40 large tumor antigen in transient heterokaryons. Mol Endocrinol 6: 837-844, 1992
Guiochon-Mantel A, Delebre K, Lescop P, Milgrom E: Nuclear localization signals also mediate the outward movement of proteins from the nucleus. Proc Natl Acad Sci USA 91: 7179-7183, 1994
Tyagi RK, Amazit L, Lescop P, Milgrom E, 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: 1684-1695, 1998
Liu J, DeFranco DB: Protracted nuclear export of the glucocorticoid receptor limits its turnover and does not require the exportin 1/CRMI-directed nuclear export pathway. Mol Endocrinol 14: 40-51, 2000
Black BE, Holaska JM, Rastinejad F, Paschal BM: DNA binding domains in diverse nuclear receptors function as nuclear export signals. Curr Biol 11: 1749-1758, 2001
Smith CL: Cross-talk between peptide growth factor and estrogen signaling pathways. Biol Rep 58: 627-632, 1998
Bunone G, Briand PA, Milsicek RJ, Picard D: Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. EMBO J 15: 2174-2183, 1996
Kato S, Endoh H, Masuhiro Y, Kitamoto T, Uchiyama S, Sasaki H, Masushigae S, Gotoh Y, Nishida E, Kawashima H, Metzger D, Chambon P: Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase. Science 270: 1491-1494, 1995
Rogatsky I, Trowbridge JM, Garabedian MJ: Potentiation of human estrogen receptor transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex. J Biol Chem 274: 22296-22302, 1999
Migliaccio A, Di Domenico M, Castoria G, de Falco A, Bontempo P, Nola E, Auricchio FF: Tyrosine kinase/p21ras/MAP-kinase pathway activation by estradiol-receptor complex in MCF-7 cells. EMBO J 15: 1292-1300, 1996
Chen D, Pace PE, Coombes C, Ali S: Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization. Mol Cell Biol 19: 1002-1015, 1999
Joel PB, Smith J, Sturgill T, Fisher TL, Blenis J, Lannigan D. A: pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167. Mol Cell Biol 18: 1978-1984, 1998
Arnold SF, Obourn JD, Jaffe H, Notides AC: Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. Mol Endocrinol 8: 1208-1214, 1994
Goff P, Montano MM, Schodin DJ, Katzenellenbogen BS: Phosphorylation of the human estrogen receptor: Identification of hormone regulated sites and examination of their influence on transcriptional activity. J Biol Chem 269: 4458-4466, 1994
Onate SA, Boonyaratanakornkit V, Spencer TE, Tsai SY, Tsai MJ, Edwards DP, O'Malley BW: The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J Biol Chem 273: 12101-12108, 1998
Suen CS, Berrodin TJ, Mastroeni R, Cheskis BJ, Lyttle CR, Frail DE: A transcriptional coactivator, steroid receptor coactivator-3, selectively augments steroid receptor transcriptional activity. J Biol Chem 273: 27645-27653, 1998
Lee H, Jiang F, Wang Q, Nicosia SV, Yang JS, Bai W: MEKK1 activation of human estrogen receptor α and stimulation of the agonistic activity of 4-hydroxytamoxifen in endometrial and ovarian cancer cells. Mol Endocrinol 14: 1882-1896, 2000
Lee H, Bai W: Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation. Mol Cell Biol 22: 5835-5845, 2002
Razandi M, Pedram A, Levin ER: Estrogen signals to the preservation of endothelial cell form and function. J Biol Chem 275: 38540-38546, 2000
Engel K, Kotlyarov A, Gaestel M: Leptomycin B-sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation. EMBO J 17: 3363-3371, 1998
del Arco PG, Martinez-Martinez S, Maldonado JL, Ortega-Perez I, Redondo JM: A role for the p38 MAP kinase pathway in the nuclear shuttling of NFATp. J Biol Chem 275: 13872-13878, 2000
Bulavin DV, Saito S, Hollander MC, Sakaguchi K, Anderson CW, Apella E, Fornace AJ Jr: Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO J 18: 6845-6854, 1999
Zhang Y, Xiong Y: A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation. Science 292: 1910-1915, 2001
Liu J, DeFranco DB: Chromatin recycling of glucocorticoid receptors: Implications for multiple roles of heat shock protein 90. Mol Endocrinol 13: 355-365, 1999
Sebastian T, Thampan RV: Nuclear estrogen receptor II(nERII) is involved in the estrogen dependent ribonucleoprotein transport in the goat uterus: I Localization of nERII in snRNP. J Cell Biochem 84: 217-226, 2002a
Sebastian T, Thampan RV: Nuclear estrogen receptor II(nERII) is involved in the estrogen dependent ribonucleoprotein transport in thegoat uterus: II Isolation and characterization of three snRNP proteins which bind to nERII. J Cell Biochem 84: 226-236, 2002b
Nirmala PB, Thampan RV: Ubiquitination of the rat uterine estrogen receptor: Dependence on estradiol. Biochem Biophys Res Commun 213: 24-31, 1995c
Nawaz Z, Lonard DM, Dennis AP, Smith CL, O'Malley BW: Proteasome-dependent degradation of the human estrogen receptor. Proc Natl Acad Sci USA 96: 1858-1862, 1999
Thampan RV: The nuclear binding of estradiol stimulates ribonucleoprotein transport in the rat uterus. J Biol Chem 260: 5420-5426, 1985
Thampan RV: Estradiol-stimulated nuclear ribonucleoprotein transport in the rat uterus: A molecular basis. Biochemistry 27: 5019-5026, 1988
Vazquez-Nin GH, Echeverria OM, Fakan S, Traish AM, Wotiz HH, Martin TE: Immunoelectron microscopic localization of estrogen receptor on pre-mRNA containing constituents of rat uterine cell nuclei. Exp Cell Res 192: 396-404, 1991
Heap RB, Symons AM, Watkins JC: Steroids and their interactions with phospholipids: Solubility, distribution co-efficient and effect on potassium permeability of liposomes. Biochim Biophys Acta 218: 482-495, 1970
Lawrence DK, Gill EW: Structurally specific effects of some steroid anesthetics on spin labeled liposomes. Mol Pharmacol 11: 280-286, 1974
Karthikeyan N, Thampan RV: Plasma membrane is the primary site of localization of the non-activated estrogen receptor in the goat uterus: Hormone binding causes receptor internalization. Arch Biochem Biophys 325: 47-57, 1996
Jaya, P, Thampan RV: A nuclear transforming factor that converts the goat uterine non-activated estrogen receptor (naER) to nuclear estrogen receptor II (nER-II). Prot Exp Purific 20: 347-356, 2000
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Sebastian, T., Sreeja, S. & Thampan, R.V. Import and export of nuclear proteins: Focus on the nucleocytoplasmic movements of two different species of mammalian estrogen receptor. Mol Cell Biochem 260, 91–102 (2004). https://doi.org/10.1023/B:MCBI.0000026060.81570.35
Issue Date:
DOI: https://doi.org/10.1023/B:MCBI.0000026060.81570.35