MECHANISMS CONTROLLING STEROID-RECEPTOR BINDING TO SPECIFIC DNA-SEQUENCES

被引：28

作者：

EDWARDS, DP

DEMARZO, AM

ONATE, SA

BECK, CA

ESTES, PA

NORDEEN, SK

机构：

[1] Department of Pathology, University of Colorado Health Sciences Center, Denver, CO

来源：

STEROIDS | 1991年 / 56卷 / 05期

关键词：

STEROIDS; PROGESTERONE RECEPTORS; HORMONE-RESPONSE ELEMENTS; DNA BINDING; RECEPTOR DIMERIZATION; BREAST CANCER;

D O I：

10.1016/0039-128X(91)90046-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Mammalian progesterone receptors activated by hormone binding in nuclei of intact cells exhibit substantially higher binding activity for specific DNA sequences than receptors bound with hormone and activated in cell-free cytosol. Differences in DNA-binding activity occur despite the fact that both activated receptor forms sediment at 4S on sucrose gradients and are apparently dissociated from the heat shock protein 90. This suggests that hormone-induced release of heat shock protein 90 from receptors is necessary, but not sufficient for maximal activation of DNA binding. This report is a review of studies from our laboratories that have examined the role of receptor interaction with other nuclear protein factor(s), and receptor dimerization in solution, as additional regulatory steps involved in the process of receptor activation and binding to specific gene sequences.

引用

页码：271 / 278

页数：8

共 39 条

[1]

Evans, The steroid and thyroid hormone receptor superfamily, Science, 240, pp. 889-895, (1988)

[2]

Beato, Gene regulation by steroid hormones, Cell, 56, pp. 335-344, (1989)

[3]

Pratt, Sanchez, Bresnick, Meshinchi, Scherrer, Dalman, Welsh, Interaction of the glucocorticoid receptor with the M<sub>r</sub> 90,000 heat shock protein: an evolving model of ligand-mediated receptor transformation and translocation, Cancer Res, 49, pp. 2222s-2229s, (1989)

[4]

Schuh, Yonemoto, Brugge, Bauer, Riehl, Sullivan, Toft, A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60<sup>v-src</sup>, J Biol Chem, 260, pp. 14292-14296, (1985)

[5]

Sanchez, Toft, Schlesinger, Pratt, Evidence that the 90-kDa phosphoprotein associated with the untransformed glucocorticoid receptor is a murine heat shock protein, J Biol Chem, 260, pp. 12398-12401, (1985)

[6]

Kost, Smith, Sullivan, Welch, Toft, Binding of heat shock proteins to the avian progesterone receptor, Mol Cell Biol, 9, pp. 3829-3838, (1989)

[7]

Sanchez, Meshinchi, Schlesinger, Pratt, Demonstration that the 90 kilodalton heat shock protein is bound to the glucocorticoid receptor in its 9S nondeoxynucleic acid binding form, Mol Endocrinol, 1, pp. 908-912, (1987)

[8]

Sanchez, Meshinchi, Tienrungroj, Schlesinger, Toft, Pratt, Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor, J Biol Chem, 262, pp. 6986-6991, (1987)

[9]

Mendel, Bodwell, Gametchu, Harrison, Munck, Molybdate-stabilized nonactivated glucocorticoid receptor complexes contain a 90 kDa non-steroid binding phosphoprotein that is lost on activation, J Biol Chem, 261, pp. 3758-3768, (1986)

[10]

Denner, Weigel, Schrader, O'Malley, Hormone-dependent regulation of chicken progesterone receptor deoxyribonucleic acid binding and phosphorylation, Endocrinology, 125, pp. 3051-3058, (1989)

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