The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein.
Open accessAbstract
Untransformed cytosol receptors for progesterone (PR), androgen (AR), estrogen (ER), and glucocorticosteroid (GR) in rabbit tissues contain a 59-kDa protein (p59) (Tai, P.K.K., Maeda, Y., Nakao, K., Wakim, N.G., Duhring, J.L., and Faber, L.E. (1986) Biochemistry 25, 5269-5275) and a 90-kDa heat shock protein (hsp90). In the present study, receptors from calf uterus (PR, AR, ER, and GR) and from human breast cancer MCF7 cells (PR and GR) were also shown to be comprised of hsp90 and p59. These heterooligomer receptor complexes were stabilized both by transition metal oxyanions (molybdate and tungstate) and chemical cross-linking with dimethylpimelimidate. In 0.4 M KCl, tungstate-stabilized (but not molybdate-stabilized) PR, AR, ER, and GR retained hsp90, but lost p59. Dimethylpimelimidate cross-linking prevented p59 dissociation from hsp90-receptor complexes. Stabilization with tungstate and/or cross-linking permitted immunoaffinity purification of untransformed rabbit as well as calf PR and ER on EC1-Affi-Gel 10 column (an anti-p59 immunoadsorbant). Combined immunoaffinity purification and cross-linking experiments indicated that p59 is bound to hsp90 in the cytosol. We propose that in the nontransformed steroid receptor, p59 interacts with hsp90 rather than with the hormone binding subunit.
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Cites
A 59-kilodalton protein associated with progestin, estrogen, androgen and glucocorticoid receptors
Tai, P. K. K., Maeda, Y., Nakao, K., Wakim, N. G., Duhring, J. L., & Faber, L. E. (1986) · Biochemistry · doi:10.1021/bi00366a043 · Cited by 257
Cited by
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*
Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791
The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
Riggs, D. L., Roberts, P. J., Chirillo, S. C., Cheung‐Flynn, J., Prapapanich, V., Ratajczak, T., Gaber, R., Picard, D., & Smith, D. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg108 · Cited by 353
Binding of p23 and hsp90 during assembly with the progesterone receptor.
Johnson, J. L., & Toft, D. O. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.6.8592513 · Cited by 233
HSP56: a novel heat shock protein associated with untransformed steroid receptor complexes
Sanchez, E. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45667-0 · Cited by 214
Veldscholte, J., Berrevoets, C. A., Zegers, N. D., Van der Kwast, T. H., Grootegoed, J. A., & Mulder, E. (1992) · Biochemistry · doi:10.1021/bi00147a029 · Cited by 139
Metadata
- Authors
- Renoir, J. M., Radanyi, C., Faber, L. E., & Baulieu, E. E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-06
- Volume
- 265
- Issue
- 18
- Pages
- 10740-10745
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1550188105
- Cited by
- 174
- References
- 1
- FWCI
- 7.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Renoir, J. M., Radanyi, C., Faber, L. E., & Baulieu, E. E. (1990). The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)87009-0
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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