ArticleGenes & development2000
The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies.
Article in Genes & development, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
57 citing papers in PubMed, 167 citations in OpenAlex.
- p23 protects against ferroptosis of brain microvascular endothelial cells in ischemic stroke.International journal of molecular medicine · 2025Article
- Organismal Roles of Hsp90.Biomolecules · 2023Review
- Selective vulnerabilities in the proteostasis network of castration-resistant prostate cancer.Cell chemical biology · 2022Article
- Article
- Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.Nature communications · 2021Article
- The Nuclear and DNA-Associated Molecular Chaperone Network.Cold Spring Harbor perspectives in biology · 2019Review
- Characterization of an Hsp90-Independent Interaction between Co-Chaperone p23 and Transcription Factor p53.Biochemistry · 2018Article
- The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease.International journal of molecular sciences · 2017Review
- The HSP90 chaperone machinery.Nature reviews. Molecular cell biology · 2017Review
- Article
- Article
- The Interactome of the Glucocorticoid Receptor and Its Influence on the Actions of Glucocorticoids in Combatting Inflammatory and Infectious Diseases.Microbiology and molecular biology reviews : MMBR · 2016Review
- A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation.Molecular and cellular biology · 2016Article
- HSP90AB1: Helping the good and the bad.Gene · 2016Review
- Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Nature communications · 2015Article
- Co-chaperone p23 regulates C. elegans Lifespan in Response to Temperature.PLoS genetics · 2015Article
- Modulation of the maladaptive stress response to manage diseases of protein folding.PLoS biology · 2014Article
- Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.Nature structural & molecular biology · 2013Article
- Molecular cochaperones: tumor growth and cancer treatment.Scientifica · 2013Review
- The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status.Molecular cell · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multiple molecular chaperones, including Hsp90 and p23, interact with members of the intracellular receptor (IR) family. To investigate p23 function, we compared the effects of three p23 proteins on IR activities, yeast p23 (sba1p) and the two human p23 homologs, p23 and tsp23. We found that Sba1p was indistinguishable from human p23 in assays of seven IR activities in both animal cells and in yeast; in contrast, certain effects of tsp23 were specific to that homolog. Transcriptional activation by two IRs was increased by expression of any of the p23 species, whereas activation by five other IRs was decreased by Sba1p or p23, and unaffected by tsp23. p23 was expressed in all tissues examined except striated and cardiac muscle, whereas tsp23 accumulated in a complementary pattern; hence, p23 proteins might contribute to tissue-specific differences in IR activities. Unlike Hsp90, which acts on IR aporeceptors to stimulate ligand potency (i.e., hormone-binding affinity), p23 proteins acted on IR holoreceptors to alter ligand efficiencies (i.e., transcriptional activation activity). Moreover, the p23 effects developed slowly, requiring prolonged exposure to hormone. In vitro, p23 interacted preferentially with hormone-receptor-response element ternary complexes, and stimulated receptor-DNA dissociation. The dissociation was reversed by addition of a fragment of the GRIP1 coactivator, suggesting that the two reactions may be in competition in vivo. Our findings suggest that p23 functions at one or more late steps in IR-mediated signal transduction, perhaps including receptor recycling and/or reversal of the response.
Indexed as
Identifiers
10691735PMC316379W2156437614What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.