ArticleCell cycle (Georgetown, Tex.)2012
The expanding proteome of the molecular chaperone HSP90.
Article in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- The N6-methyladenosine reader IGF2BP3 promotes bladder cancer progression through enhancing HSP90AB1 expression.The FEBS journal · 2025Article
- Discovery of potent heat shock protein 90 (Hsp90) inhibitors: structure-based virtual screening, molecular dynamics simulation, and biological evaluation.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Native Size-Exclusion Chromatography-Based Mass Spectrometry Reveals New Components of the Early Heat Shock Protein 90 Inhibition Response Among Limited Global Changes.Molecular & cellular proteomics : MCP · 2023Article
- Article
- Regulation of ClC-2 Chloride Channel Proteostasis by Molecular Chaperones: Correction of Leukodystrophy-Associated Defect.International journal of molecular sciences · 2021Article
- HSP90 Inhibition and Modulation of the Proteome: Therapeutical Implications for Idiopathic Pulmonary Fibrosis (IPF).International journal of molecular sciences · 2020Review
- Inhibition of Embryonic HSP 90 Function Promotes Variation of Cold Tolerance in Zebrafish.Frontiers in genetics · 2020Article
- Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90β.Scientific reports · 2016Article
- Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.Cell chemical biology · 2016Review
- Article
- HSP90 empowers evolution of resistance to hormonal therapy in human breast cancer models.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Gα12 structural determinants of Hsp90 interaction are necessary for serum response element-mediated transcriptional activation.Molecular pharmacology · 2014Article
- Optical and radioiodinated tethered Hsp90 inhibitors reveal selective internalization of ectopic Hsp90 in malignant breast tumor cells.Chemistry & biology · 2013Article
- The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors.Journal of proteome research · 2013Article
- LPS induces pp60c-src-mediated tyrosine phosphorylation of Hsp90 in lung vascular endothelial cells and mouse lung.American journal of physiology. Lung cellular and molecular physiology · 2013Article
- Hsp90, an unlikely ally in the war on cancer.The FEBS journal · 2013Review
- Molecular biology: Choose your protein partners.Nature · 2012Article
- HSP90 Inhibitor Geldanamycin as a Radiation Response Modificator in Human Blood Cells.Dose-response : a publication of International Hormesis SocietyArticle
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The molecular chaperone HSP90 maintains the activity and stability of a diverse set of "client" proteins that play key roles in normal and disease biology. Around 20 HSP90 inhibitors that deplete the oncogenic clientele have entered clinical trials for cancer. However, the full extent of the HSP90-dependent proteome, which encompasses not only clients but also proteins modulated by downstream transcriptional responses, is still incompletely characterized and poorly understood. Earlier large-scale efforts to define the HSP90 proteome have been valuable but are incomplete because of limited technical sensitivity. Here we discuss previous large-scale surveys of proteome perturbations induced by HSP90 inhibitors in light of a significant new study using state-of-the-art SILAC technology combined with more sensitive high-resolution mass spectrometry (MS) that extends the catalog of proteomic changes in inhibitor-treated cancer cells. Among wide-ranging changes, major functional responses include downregulation of protein kinase activity and the DNA damage response alongside upregulation of the protein degradation machinery. Despite this improved proteomic coverage, there was surprisingly little overlap with previous studies. This may be due in part to technical issues but is likely also due to the variability of the HSP90 proteome with the inhibitor conditions used, the cancer cell type and the genetic status of client proteins. We suggest future proteomic studies to address these factors, to help distinguish client protein components from indirect transcriptional components and to address other key questions in fundamental and translational HSP90 research. Such studies should also reveal new biomarkers for patient selection and novel targets for therapeutic intervention.
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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.