A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex
- PMID: 1373296
- DOI: 10.1016/0960-0760(92)90348-m
A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex
Abstract
It has recently been reported that incubation of avian progesterone receptors, mouse glucocorticoid receptors, or the viral tyrosine kinase pp60src with rabbit reticulocyte lysate reconstitutes their association with the 90 kDa heat shock protein, hsp90. The reassociation is thought to require unfolding of the steroid receptor or pp60src before hsp90 can bind. The unfoldase activity may be provided by hsp70, which is also present in the reconstituted receptor heterocomplex. In this paper we review evidence that hsp70 and hsp90 are associated in cytosolic heterocomplexes that contain a limited number of other proteins. From an analysis of known receptor-hsp interactions and a predicted direct interaction between hsp90 and hsp70 we have developed an admittedly very speculative model of glucocorticoid receptor unfolding and stabilization. One important feature of the model is that the receptor becomes attached to a heat shock protein heterocomplex rather than undergoing independent unfolding and stabilization events. The model requires that hsp70 and hsp90 bind directly to the receptor at independent sites. Importantly, the model accommodates the stoichiometry of 2 hsp90 per 1 molecule of receptor that has been assayed in the untransformed GR heterocomplex in cytosols prepared from hormone-free cells.
Similar articles
-
The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor.J Biol Chem. 1995 Sep 1;270(35):20479-84. doi: 10.1074/jbc.270.35.20479. J Biol Chem. 1995. PMID: 7657624
-
The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex.J Biol Chem. 1998 Mar 27;273(13):7358-66. doi: 10.1074/jbc.273.13.7358. J Biol Chem. 1998. PMID: 9516432
-
Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90.J Biol Chem. 1994 Feb 18;269(7):5043-9. J Biol Chem. 1994. PMID: 8106480
-
Regulation of glucocorticoid receptor function through assembly of a receptor-heat shock protein complex.Ann N Y Acad Sci. 1993 Jun 11;684:35-48. doi: 10.1111/j.1749-6632.1993.tb32269.x. Ann N Y Acad Sci. 1993. PMID: 8317846 Review.
-
The relationship between glucocorticoid receptor binding to Hsp90 and receptor function.Nihon Naibunpi Gakkai Zasshi. 1990 Dec 20;66(12):1185-97. doi: 10.1507/endocrine1927.66.12_1185. Nihon Naibunpi Gakkai Zasshi. 1990. PMID: 2292310 Review.
Cited by
-
Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins.Mol Cell Biol. 1998 Jun;18(6):3330-9. doi: 10.1128/MCB.18.6.3330. Mol Cell Biol. 1998. PMID: 9584173 Free PMC article.
-
Achieving Endo/Lysosomal Escape Using Smart Nanosystems for Efficient Cellular Delivery.Molecules. 2024 Jul 1;29(13):3131. doi: 10.3390/molecules29133131. Molecules. 2024. PMID: 38999083 Free PMC article. Review.
-
Heat shock proteins: molecular chaperones of protein biogenesis.Microbiol Rev. 1993 Jun;57(2):402-14. doi: 10.1128/mr.57.2.402-414.1993. Microbiol Rev. 1993. PMID: 8336673 Free PMC article. Review.
-
The orphan receptors NGFI-B and steroidogenic factor 1 establish monomer binding as a third paradigm of nuclear receptor-DNA interaction.Mol Cell Biol. 1993 Sep;13(9):5794-804. doi: 10.1128/mcb.13.9.5794-5804.1993. Mol Cell Biol. 1993. PMID: 8395013 Free PMC article.
-
In vivo analysis of the Hsp90 cochaperone Sti1 (p60).Mol Cell Biol. 1997 Jan;17(1):318-25. doi: 10.1128/MCB.17.1.318. Mol Cell Biol. 1997. PMID: 8972212 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
