Multimeric forms of members of the steroid/thyroid superfamily of receptors with the ultraspiracle receptor
Patent 6281330 Issued on August 28, 2001. Estimated Expiration Date: August 28, 2018. Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.
In accordance with the present invention, it has been discovered that various members of the steroid/thyroid superfamily of receptors can interact with the insect-derived ultraspiracle receptor, to form multimeric species. Accordingly, the interaction of at least one member of the steroid/thyroid superfamily of receptors with at least the dimerization domain of the ultraspiracle receptor modulates the ability of said member of the steroid/thyroid superfamily of receptors to transactivate transcription of genes maintained under hormone expression control in the presence of the cognate ligand for said member of the superfamily.
Other References
Yao et al., "DNA Binding Properties of Ultraspiracle, the Drosophila Retinoid X Receptor Homologue" Journal of Cellular Biochemistry--Keystone Symposia on Molecular & Cellular Biology, Supplement 16, p. 90, Abstract W219, (Apr. 3-16, 1992)
Yao et al., "Drosophila ultraspiracle Modulates Ecdysone Receptor Function via Heterodimer Formation" Cell 71:63-72 (1992)
Thomas et al., "Heterodimeriztion of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle" Nature 362:471-475 (1993)
Geoff Richards "Switching partners?" Current Biology 2(12):657-659 (1992)
Christianson et al., "DNA binding and heteromerization of the Drosophila transcription factor chorion factor 1/ultraspiracle" Proc. Natl. Acad. Sci. USA 89:11503-11507 (1992)
Cherbas, et al., Biosynthesis, Metabolism and Mode of Action of Invertebrate Hormones, 305-22, 1984.
Oro, et al, Development, vol. 115, 449-62 (1992).
Kumar and Chambon, "The Estrogen Receptor Binds Tightly to Its Responsive Element as a Ligand-Induced Homodimer", Cell vol. 55:145-156 (1988)
Tsai et al., "Molecular Interactions of Steroid Hormone Receptor with Its Enhancer Element: Evidence for Receptor Dimer Formation", Cell vol. 55:361-369 (1988)
Murray and Towle, "Identification of Nuclear Factors that Enhance Binding of the Thyroid Hormone Receptor to a Thyroid Hormone Response Element", Molecular Endocrinology vol. 3:1434-1442 (1989)
Glass et al., "Multiple Cell Type-Specific Proteins Differentially Regulate Target Sequence Recognition by the Retinoic Acid Receptor", Cell vol. 63:729-738 (1990)
Liao et al., "Vitamin D receptor interaction with specific DNA requires a nuclear protein and 1,25-dihydroxyvitamin D3 ", Proc. Natl. Acad. Sci. USA vol. 87:9751-9755 (1990)
Leid et al., "Purification, Cloning, and RXR Identity of the HeLa Cell Factor with Which RAR or TR Heterodimerizes to Bind Target Sequences Efficiently", Cell vol. 68:377-395 (1992)
Yu et al., RXRଲ: A Coregulator That Enhances Binding of Retinoic Acid, Thyroid Hormone, and Vitamin D Receptors to Their Cognate Response Elements, Cell vol. 67:1251-1266 (1991)
Kliewer et al., "Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling", Nature vol. 355:446-449 (1992)
Zhang et al., "Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors", Nature vol. 355:441-446 (1992)
Cherbas et al., "The Action of Ecdysone in Imaginal Discs and KcCells of Drosophila melanogaster"Biosynthesis, metabolism and mode of action of invertebrate hormones, (ed. J Hoffman & M. Porchet pp. 305-322 Springer-Verlag, Berlin, 1984)
Koelle et al., "The Drosophila EcR Gene Encodes an Ecdysone Receptor, a New Member of the Steroid Receptor Superfamily", Cell vol. 67:59-77 (1991)
Kunkel, Thomas A., "Rapid and efficient site-specific mutagenesis without phenotypic selection", Proc. Natl. Acad. Sci. USA vol. 82:488-492 (1985)
Soeller et al., "In vitro transcription of the Drosophila engrailed gene", Genes & Development vol. 2:68-81 (1988)
Kliewer et al., "Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors", Nature vol. 358:771-774 (1992)
Noda et al., "Identification of a DNA sequence responsible for binding of the 1,25-dihydroxyvitamin D3 receptor and 1,25-dihydroxyvitamin D3 enhancement of mouse secreted phosphoprotein 1 (Spp-1 or osteopontin) gene expression", Proc. Natl. Acad. Sci. USA vol. 87:9995-9999 (1990)
Sap et al., "Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product", Nature vol. 340:242-244 (1989)
Forman et al., "A Domain Containing Leucine-Zipper-Like Motifs Mediate Novel in vivo Interactions between the Thyroid Hormone and Retinoid Acid Receptors", Molecular Endocrinology vol. 3:1610-1626 (1989)
Fawell et al., "Characterization and Colocalization of Steroid Binding and Dimerization Activities in the Mouse Estrogen Receptor", Cell vol. 60:953-962 (1990)
Riddihough and Pelham, "An ecdysone response element in the Drosophila hsp27 promoter", The EMBO Journal vol. 6:3729-3734 (1987)
Richards, Geoff, "The Radioimmune Assay of Ecdysteroid Titres in Drosophila melanogaster", Molecular and Cellular Endocrinology vol. 21:181-197 (1981)
Oro et al., The Drosophila retinoid X receptor homolog ultraspiracle functions in both female reproduction and eye morphogenesis, Development vol. 115:449-462 (1992)
Yang et al., "Characterization of DNA binding and retinoic acid binding properties of retinoic acid receptor", Proc. Natl. Acad. Sci. USA vol. 88:3559-3563 (1991)
Damm et al., "Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist", Nature vol. 339:593-597 (1989)
Sucov et al., "Characterization of an autoregulated response element in the mouse retinoic acid receptor type ଲ gene", Proc. Natl. Acad. Sci. USA vol. 87:5392-5396 (1990)
de The et al., "Identification of a retinoic acid responsive element in the retinoic acid receptor ଲ gene", Nature vol. 343:177-180 (1990)
Thompson and Evans, "Trans-activation by thyroid hormone receptors: Functional parallels with steroid hormone receptors", Proc. Natl. Acad. Sci. USA vol. 86:3494-3498 (1989)
Issemann and Green, "Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators", Nature vol. 347:645-650 (1990)
Oro et al., "Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor", Nature vol. 347:298-301 (1990)
Evans, Ronald M., "The Steroid and Thyroid Hormone Receptor Superfamily", Science vol. 240:889-895 (1988)
Vaughan et al., "Detection and Purification of Inhibin Using Antisera Generated against Synthetic Peptide Fragments", Methods in Enzymology vol. 168:588-617 (1989)
Mangelsdorf et al., "Nuclear receptor that identifies a novel retinoic acid response pathway", Nature vol. 345:224-229 (1990)
Sladek et al., "Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily", Genes & Development vol. 4:2353-2365 (1990)
Miyajima et al., "Identification of two novel members of erbA superfamily by molecular cloning: the gene products of the two are highly related to each other", Nucleic Acids Research vol. 16:11057-11074 (1988)
Wang et al., "COUP transcription factor is a member of the steroid receptor superfamily", Nature vol. 340:163-166 (1989)
Mlodzik et al., "The Drosophila seven-up Gene, a Member of the Steroid Receptor Gene Superfamily, Controls Photoreceptor Cell Fates", Cell vol. 60:211-224 (1990)
Ladias and Karathanasis, "Regulation of the Apolipoprotein AI Gene by ARP-1, a Novel Member of the Steroid Receptor Superfamily", Science vol. 251:561-565 (1991)
Umesone et al., "Direct Repeats as Selective Response Elements for the Thyroid Hormone, Retinoic Acid, and Vitamin D3 Receptors", Cell vol. 65:1255-1266 (1991)
Hollenberg and Evans, "Multiple and Cooperative trans-Activation Domains of the Human Glucocorticoid Receptor", Cell vol. 55:899-906 (1988)
Giguere et al., "Identification of a receptor for the morphogen retinoic acid", Nature vol. 330:624-629 (1987)
Umesono et al., "Retinoic acid and thyroid hormone induce gene expression through a common responsive element", Nature vol. 336:262-265 (1988)
Cherbas et al., "Identification of ecdysone response elements by analysis of the Drosophila Eip28/29 gene", Genes & Development vol. 5:120-131 (1991