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Science 13 December 1991:
Vol. 254. no. 5038, pp. 1636 - 1639
DOI: 10.1126/science.1749936

Articles

Science, Vol 254, Issue 5038, 1636-1639
Copyright © 1991 by American Association for the Advancement of Science


articles

Dopaminergic and ligand-independent activation of steroid hormone receptors

RF Power, SK Mani, J Codina, OM Conneely, and BW O'Malley

Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.

The current view of how steroid hormone receptors affect gene transcription is that these receptors, on binding ligand, change to a state in which they can interact with chromatin and regulate transcription of target genes. Receptor activation is believed to be dependent only on this ligand-binding event. Selected steroid hormone receptors can be activated in a ligand-independent manner by a membrane receptor agonist, the neurotransmitter dopamine. In vitro, dopamine faithfully mimicked the effect of progesterone by causing a translocation of chicken progesterone receptor (cPR) from cytoplasm to nucleus. Dual activation by progesterone and dopamine was dissociable, and a serine residue in the cPR was identified that is not necessary for progesterone-dependent activation of cPR, but is essential for dopamine activation of this receptor.


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Protein Phosphatases 1 and 2A Regulate the Transcriptional and DNA Binding Activities of Retinoic Acid Receptors.
P. Lefebvre, M.-P. Gaub, A. Tahayato, Céc. Rochette-Egly, and P. Formstecher (1995)
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Convergent pathways for steroid hormone- and neurotransmitter-induced rat sexual behavior.
S. Mani, J. Allen, J. Clark, J. Blaustein, and B. O'Malley (1994)
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The antiestrogen ICI 182780 disrupts estrogen receptor nucleocytoplasmic shuttling.
S Dauvois, R White, and M. Parker (1993)
J. Cell Sci. 106, 1377-1388
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Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex.
P. Tai, M. Albers, H Chang, L. Faber, and S. Schreiber (1992)
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G. Urban, T. Golden, I. V. Aragon, J. G. Scammell, N. M. Dean, and R. E. Honkanen (2001)
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