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Genetic and Biochemical Analysis of p23 and Ansamycin Antibiotics in the Function of Hsp90-Dependent Signaling Proteins

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Bohen, Sean P.·1998·Molecular and Cellular Biology

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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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A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae.
Sikorski, R. S., & Hieter, P. (1989) · Genetics · doi:10.1093/genetics/122.1.19 · Cited by 8,590
The Steroid and Thyroid Hormone Receptor Superfamily
Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,394
Getting started with yeast
Sherman, F. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)94004-v · Cited by 4,078
Improved method for high efficiency transformation of intact yeast cells.
Gietz, D., Jean, A. S., Woods, R. A., & Schiestl, R. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.6.1425 · Cited by 3,379
STEROID RECEPTOR REGULATED TRANSCRIPTION OF SPECIFIC GENES AND GENE NETWORKS
Yamamoto, K. R. (1985) · Annual Review of Genetics · doi:10.1146/annurev.ge.19.120185.001233 · Cited by 1,850
Multifunctional yeast high-copy-number shuttle vectors
Christianson, T., Sikorski, R. S., Dante, M., Shero, J. H., & Hieter, P. (1992) · Gene · doi:10.1016/0378-1119(92)90454-w · Cited by 1,660
Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent
Stebbins, C. E., Russo, A. A., Schneider, C. B., Rosen, N. X., Hartl, F. U., & Pavletich, N. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80203-2 · Cited by 1,370
Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone
Prodromou, C., Roe, S. M., O’Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1997) · Cell · doi:10.1016/s0092-8674(00)80314-1 · Cited by 1,258
The Biology of heat shock proteins and molecular chaperones.
Morimoto, R. I., Tissieres, A., & Georgopoulos, C. P. (1994) · Cited by 1,244

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10.1128/mcb.9.9.3919-3930.1989 · DOI · Paper page
10.1128/mcb.14.3.1956-1963.1994 · DOI
10.1128/mcb.4.12.2802-2810.1984 · DOI
10.1128/mcb.13.9.5290-5300.1993 · DOI

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Authors: Bohen, S. P.
Affiliations: National Institutes of Health (US)
Corresponding author: Bohen, Sean P.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1998-06
Volume: 18
Issue: 6
Pages: 3330-3339
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.18.6.3330
PMC: PMC108914
OpenAlex: W1827557434
Cited by: 106
References: 70
Citations by year: 2024: 1 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 3
FWCI: 3.72
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute for Health and Care Research
National Institutes of Health
National Cancer Institute
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: HSP90, p23, ansamycin antibiotics, steroid hormone receptors, molecular chaperones, ligand binding, protein maturation
MeSH terms: Amino Acid Sequence, Anti-Bacterial Agents, Antibiotics, Antineoplastic, DNA-Binding Proteins, Humans, Molecular Sequence Data, Phenotype, Protein-Tyrosine Kinases, Quinones, Receptors, Steroid, Saccharomyces cerevisiae, Signal Transduction, Oncogene Protein pp60(v-src), Benzoquinones, Sequence Alignment, HSP90 Heat-Shock Proteins, Lactams, Macrocyclic

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Genetic and Biochemical Analysis of p23 and Ansamycin Antibiotics in the Function of Hsp90-Dependent Signaling Proteins

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