ArticleProceedings of the National Academy of Sciences of the United States of America2015
Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 85 citations in OpenAlex.
- Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome.Cell stress & chaperones · 2026Article
- Disruption of HSPA8-GEMIN5 interaction suppresses colorectal cancer by impaired splicing-translation coupling-mediated proteostasis imbalance.Journal of experimental & clinical cancer research : CR · 2026Article
- Beyond Folding: Expanding the Functional Landscape of Hsp90 Chaperone Machinery in Health and Disease.International journal of molecular sciences · 2025Review
- The known unknowns of the Hsp90 chaperone.eLife · 2024Review
- Insights into the Allosteric Regulation of Human Hsp90 Revealed by NMR Spectroscopy.Biomolecules · 2024Review
- The role of the co-chaperone HOP in plant homeostasis during development and stress.Journal of experimental botany · 2024Review
- Molecular determinants of Hsp90 dependence of Src kinase revealed by deep mutational scanning.Protein science : a publication of the Protein Society · 2023Article
- PhosY-secretome profiling combined with kinase-substrate interaction screening defines active c-Src-driven extracellular signaling.Cell reports · 2023Article
- Structural mechanism of a drug-binding process involving a large conformational change of the protein target.Nature communications · 2023Article
- Hsp90: From Cellular to Organismal Proteostasis.Cells · 2022Review
- Hsp90 and Associated Co-Chaperones of the Malaria Parasite.Biomolecules · 2022Review
- Assembly mechanism of early Hsp90-Cdc37-kinase complexes.Science advances · 2022Article
- Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network.Science advances · 2021Article
- HSP-90/kinase complexes are stabilized by the large PPIase FKB-6.Scientific reports · 2021Article
- Hsp90-mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling.EMBO reports · 2021Article
- Distinct CDK6 complexes determine tumor cell response to CDK4/6 inhibitors and degraders.Nature cancer · 2021Article
- Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.Genetics · 2021Article
- Design of buried charged networks in artificial proteins.Nature communications · 2021Article
- Hsp90 modulates human sperm capacitation via the Erk1/2 and p38 MAPK signaling pathways.Reproductive biology and endocrinology : RB&E · 2021Article
- The Boggarts of biology: how non-genetic changes influence the genotype.Current genetics · 2021Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsp90 is a molecular chaperone involved in the activation of numerous client proteins, including many kinases. The most stringent kinase client is the oncogenic kinase v-Src. To elucidate how Hsp90 chaperones kinases, we reconstituted v-Src kinase chaperoning in vitro and show that its activation is ATP-dependent, with the cochaperone Cdc37 increasing the efficiency. Consistent with in vivo results, we find that Hsp90 does not influence the almost identical c-Src kinase. To explain these findings, we designed Src kinase chimeras that gradually transform c-Src into v-Src and show that their Hsp90 dependence correlates with compactness and folding cooperativity. Molecular dynamics simulations and hydrogen/deuterium exchange of Hsp90-dependent Src kinase variants further reveal increased transitions between inactive and active states and exposure of specific kinase regions. Thus, Hsp90 shifts an ensemble of conformations of v-Src toward high activity states that would otherwise be metastable and poorly populated.
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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.