ArticleMolecular and cellular biology1998
Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 106 citations in OpenAlex.
- 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
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation.Nature communications · 2019Article
- Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest.Cell stress & chaperones · 2015Article
- Heat shock protein 90 inhibitors repurposed against Entamoeba histolytica.Frontiers in microbiology · 2015Article
- Review
- Article
- Transgenic overexpression of p23 induces spontaneous hydronephrosis in mice.International journal of experimental pathology · 2011Article
- Detection of changes in gene regulatory patterns, elicited by perturbations of the Hsp90 molecular chaperone complex, by visualizing multiple experiments with an animation.BioData mining · 2011Article
- High levels of Hsp90 cochaperone p23 promote tumor progression and poor prognosis in breast cancer by increasing lymph node metastases and drug resistance.Cancer research · 2010Article
- Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast.Molecular biology of the cell · 2010Article
- Estrogen receptor-alpha hinge-region lysines 302 and 303 regulate receptor degradation by the proteasome.Molecular endocrinology (Baltimore, Md.) · 2008Article
- p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity.Molecular and cellular biology · 2008Article
- The heat shock protein 70 cochaperone YDJ1 is required for efficient membrane-specific flock house virus RNA replication complex assembly and function in Saccharomyces cerevisiae.Journal of virology · 2008Article
- The Hsp90 cochaperone p23 is essential for perinatal survival.Molecular and cellular biology · 2006Article
- Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.Molecular biology of the cell · 2004Article
- Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.Molecular biology of the cell · 2004Article
- Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach.Cell stress & chaperones · 2004Article
- The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin.Malaria journal · 2003Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitous molecular chaperone Hsp90 acts in concert with a cohort of associated proteins to facilitate the functional maturation of a number of cellular signaling proteins, such as steroid hormone receptors and oncogene tyrosine kinases. The Hsp90-associated protein p23 is required for the assembly of functional steroid aporeceptor complexes in cell lysates, and Hsp90-binding ansamycin antibiotics disrupt the activity of Hsp90-dependent signaling proteins in cultured mammalian cells and prevent the association of p23 with Hsp90-receptor heterocomplexes; these observations have led to the hypotheses that p23 is required for the maturation of Hsp90 target proteins and that ansamycin antibiotics abrogate the activity of such proteins by disrupting the interaction of p23 with Hsp90. In this study, I demonstrate that ansamycin antibiotics disrupt the function of Hsp90 target proteins expressed in yeast cells; prevent the assembly of Sba1, a yeast p23-like protein, into steroid receptor-Hsp90 complexes; and result in the assembly of receptor-Hsp90 complexes that are defective for ligand binding. To assess the role of p23 in Hsp90 target protein function, I show that the activity of Hsp90 target proteins is unaffected by deletion of SBA1. Interestingly, steroid receptor activity in cells lacking Sba1 displays increased sensitivity to ansamycin antibiotics, and this phenotype is rescued by the expression of human p23 in yeast cells. These findings indicate that Hsp90-dependent signaling proteins can achieve a functional conformation in vivo in the absence of p23. Furthermore, while the presence of p23 decreases the sensitivity of Hsp90-dependent processes to ansamycin treatment, ansamycin antibiotics disrupt signaling through some mechanism other than altering the Hsp90-p23 interaction.
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