ArticleCell stress & chaperones2001
Heat shock protein 90 and the nuclear transport of progesterone receptor.
Article in Cell stress & chaperones, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 22 citations in OpenAlex.
- Global signalling network analysis of luminal T47D breast cancer cells in response to progesterone.Frontiers in endocrinology · 2022Article
- Which Low-Abundance Proteins are Present in the Human Milieu of Gamete/Embryo Maternal Interaction?International journal of molecular sciences · 2019Article
- Chaperones and the maturation of steroid hormone receptor complexes.Oncotarget · 2011Article
- Hsp90 regulates the phosphorylation and activity of serum- and glucocorticoid-regulated kinase-1.The Journal of biological chemistry · 2008Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Steroid receptors exist as large oligomeric complexes in hypotonic cell extracts. In the present work, we studied the nuclear transport of the 2 major components of the oligomeric complex, the receptor itself and the heat shock protein 90 (Hsp90), by using different in vitro transport systems: digitonin permeabilized cells and purified nuclei. We demonstrate that the stabilized oligomeric complex of progesterone receptor (PR) cannot be transported into the nucleus and that unliganded PR salt dissociated from Hsp90 is transported into the nucleus. When nonstabilized PR oligomer was introduced into the nuclear transport system, the complex dissociated and the PR but not the Hsp90 was transported into the nucleus. If PR exists as an oligomeric form after synthesis, as suggested by the experiments with reticulocyte lysate, the present results suggest that the complex is short-lived and is dissociated before or during nuclear transport. Thus, the role of Hsp90 in PR action is likely to reside in the Hsp90-assisted chaperoning process of PR preceding nuclear transport of the receptor.
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