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Transformation of glucocorticoid and progesterone receptors to the DNA‐binding state

Transformation of glucocorticoid and progesterone receptors to the DNA‐binding state This brief review explores some recent observations relating to the structure of untransformed glucocorticoid and progesterone receptors and the mechanism by which the receptors are transformed to the DNA‐binding state. In their molybdate‐stabilized, untransformed state, progesterone and glucocorticoid receptors exist as a heteromeric 8‐9S complex containing one unit of steroid binding phosphoprotein and one or two units of the 90 kD heat shock protein hsp90. When the receptors are transformed, the steroid‐binding protein dissociates from hsp90. In cytosol preparations, temperature‐mediated dissociation proceeds much more rapidly in the presence of hormone. The dissociated receptor binds to DNA with high affinity, regardless of whether it is in the hormone‐bound or the hormone‐free state. These observations raise the possibility that the primary, and perhaps the only, role for the hormone is to promote dissociation of the receptor‐hsp90 complex. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Cellular Biochemistry Wiley

Transformation of glucocorticoid and progesterone receptors to the DNA‐binding state

Pratt, William B.
Journal of Cellular Biochemistry , Volume 35 (1) – Sep 1, 1987
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References (109)

Publisher
Wiley
Copyright
Copyright © 1987 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0730-2312
eISSN
1097-4644
DOI
10.1002/jcb.240350105
pmid
3312247
Publisher site
See Article on Publisher Site

Abstract

This brief review explores some recent observations relating to the structure of untransformed glucocorticoid and progesterone receptors and the mechanism by which the receptors are transformed to the DNA‐binding state. In their molybdate‐stabilized, untransformed state, progesterone and glucocorticoid receptors exist as a heteromeric 8‐9S complex containing one unit of steroid binding phosphoprotein and one or two units of the 90 kD heat shock protein hsp90. When the receptors are transformed, the steroid‐binding protein dissociates from hsp90. In cytosol preparations, temperature‐mediated dissociation proceeds much more rapidly in the presence of hormone. The dissociated receptor binds to DNA with high affinity, regardless of whether it is in the hormone‐bound or the hormone‐free state. These observations raise the possibility that the primary, and perhaps the only, role for the hormone is to promote dissociation of the receptor‐hsp90 complex.

Journal

Journal of Cellular Biochemistry – Wiley

Published: Sep 1, 1987

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