The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Role of molecular chaperones in steroid receptor action
Abstract
Unliganded steroid receptors are assembled into heterocomplexes with heat-shock protein (hsp) 90 by a multiprotein chaperone machinery. In addition to binding the receptors at the chaperone site, hsp90 binds cofactors at other sites that are part of the assembly machinery, as well as immunophilins that connect the assembled receptor-hsp90 heterocomplexes to a protein trafficking pathway. The hsp90-/hsp70-based chaperone machinery interacts with the unliganded glucocorticoid receptor to open the steroid-binding cleft to access by a steroid, and the machinery interacts in very dynamic fashion with the liganded, transformed receptor to facilitate its translocation along microtubular highways to the nucleus. In the nucleus, the chaperone machinery interacts with the receptor in transcriptional regulatory complexes after hormone dissociation to release the receptor and terminate transcriptional activation. By forming heterocomplexes with hsp90, the chaperone machinery stabilizes the receptor to degradation by the ubiquitin-proteasome pathway of proteolysis.
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Cites
Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones
Freeman, B. C., & Yamamoto, K. R. (2002) · Science · doi:10.1126/science.1073051 · Cited by 400
Galigniana, M. D., Radanyi, C., Renoir, J.-M., Housley, P. R., & Pratt, W. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010809200 · Cited by 236 · cited 2×
“The large GR–hsp90–immunophilin–dynein complexes shown in Figure 4 can be formed by incubating immunopurified aporeceptor with reticulocyte lysate, and the presence of dynein in the complexes is selectively eliminated by competition with a purified PPIase domain fragment, showing that it is the PPIase domain that link…”
BackgroundSelf-citationMorishima, Y., Murphy, P. J. M., Li, D.-P., Sanchez, E. R., & Pratt, W. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000434200 · Cited by 166 · cited 2×
“requirement that the machinery be assembled on the receptor as the individual components bind in a specific sequence to open the steroid-binding cleft during receptor–hsp90 heterocomplex assembly [13,14].”
BackgroundSelf-citationGaligniana, M. D., Harrell, J. M., Murphy, P. J. M., Chinkers, M., Radanyi, C., Renoir, J.-M., Zhang, M., & Pratt, W. B. (2002) · Biochemistry · doi:10.1021/bi020399z · Cited by 117
Self-citationThe Influence of ATP and p23 on the Conformation of hsp90
Sullivan, W. P., Owen, B. A. L., & Toft, D. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207754200 · Cited by 111 · cited 1×
“This is the conformation of hsp90 that recognizes p23, which now binds the receptor-bound hsp90 and stabilizes the GR–hsp90 heterocomplex [15].”
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Cited by
Structure and mechanism of the Hsp90 molecular chaperone machinery
Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142738 · Cited by 1,103
Lu, N. Z., & Cidlowski, J. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.025 · Cited by 455
The Hsp90 molecular chaperone: an open and shut case for treatment
Pearl, L. H., Prodromou, C., & Workman, P. (2008) · Biochemical Journal · doi:10.1042/bj20071640 · Cited by 447
Beck, I. M. E., Vanden Berghe, W., Vermeulen, L., Yamamoto, K. R., Haegeman, G., & De Bosscher, K. (2009) · Endocrine Reviews · doi:10.1210/er.2009-0013 · Cited by 298
Swe1Wee1-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function
Mollapour, M., Tsutsumi, S., Donnelly, A. C., Beebe, K., Tokita, M. J., Lee, M.-J., Lee, S., Morra, G., Bourboulia, D., Scroggins, B. T., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.005 · Cited by 196
Metadata
- Authors
- Pratt, W. B., Galigniana, M. D., Morishima, Y., & Murphy, P. J. M.
- Venue
- Essays in Biochemistry
- Publisher
- Portland Press Ltd.
- Published
- 2004-06-01
- Volume
- 40
- Pages
- 41-58
- ISSN
- 0071-1365 (ISSN-L)
- 1744-1358
- OpenAlex
- W142850513
- Cited by
- 242
- References
- 5
- FWCI
- 5.47
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
