Differential modes of activation define orphan subclasses within the steroid/thyroid receptor superfamily.
- 1 January 1992
- journal article
- Vol. 2 (3) , 273-83
Abstract
We report that three orphan receptors, hERR1, hERR2, and hTR2, members of the steroid/thyroid receptor (SR/TR) superfamily, can be activated by different ligand-independent pathways. hERR1 and hERR2 exhibit constitutive activity in the absence of exogenously added ligands. Furthermore, this constitutive activity is localized in the carboxy terminal domain of both receptors and can be transferred to other members of this superfamily using domain switch strategies. In addition, we show that hERR1 can remain constitutively active in the less evolved eukaryotic cell Saccharomyces cerevisiae. In contrast, hTR2 is not constitutively active. However, a chimera of hTR2 can be activated in a ligand-independent manner through a signal transduction pathway initiated at the cell membrane by the neurotransmitter dopamine. Like hERR1 and hERR2, hTR2 is ligand-independently activated through its carboxy terminal domain. Together, these results suggest the existence of emerging subgroups within the SR/TR superfamily that can regulate gene expression through different modes of activation.This publication has 46 references indexed in Scilit:
- 9-Cis retinoic acid stereoisomer binds and activates the nuclear receptor RXRαNature, 1992
- Interaction of the chicken progesterone receptor with heat shock protein (HSP) 90Journal of Steroid Biochemistry, 1989
- Identification of a new member of the steroid receptor super-family by cloning and sequence analysisBiochemical and Biophysical Research Communications, 1988
- A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptorCell, 1988
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- Identification of a receptor for the morphogen retinoic acidNature, 1987
- A human retinoic acid receptor which belongs to the family of nuclear receptorsNature, 1987
- Molecular Cloning of Complementary DNA Encoding the Avian Receptor for Vitamin DScience, 1987
- Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-ANature, 1986
- Human GM-CSF: Molecular Cloning of the Complementary DNA and Purification of the Natural and Recombinant ProteinsScience, 1985