ArticleProceedings of the National Academy of Sciences of the United States of America2011
Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 61 citations in OpenAlex.
- Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitors.Nature communications · 2025Article
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- The Hsp70-Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration.Cellular and molecular life sciences : CMLS · 2021Review
- Discovering protein-protein interaction stabilisers by native mass spectrometry.Chemical science · 2021Article
- Structure, Function, and Regulation of the Hsp90 Machinery.Cold Spring Harbor perspectives in biology · 2019Review
- The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones.International journal of molecular sciences · 2019Review
- Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding.Molecular & cellular proteomics : MCP · 2019Article
- Adapting to stress - chaperome networks in cancer.Nature reviews. Cancer · 2018Review
- A DNA nanoscope via auto-cycling proximity recording.Nature communications · 2017Article
- Ion Mobility-Mass Spectrometry Reveals Evidence of Specific Complex Formation between Human Histone Deacetylase 8 and Poly-r(C)-binding Protein 1.International journal of mass spectrometry · 2017Article
- Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1.eLife · 2017Article
- Quantitation of the Noncovalent Cellular Retinol-Binding Protein, Type 1 Complex Through Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- The Mechanism of Hsp90 ATPase Stimulation by Aha1.Scientific reports · 2016Article
- The interchange of immunophilins leads to parallel pathways and different intermediates in the assembly of Hsp90 glucocorticoid receptor complexes.Cell discovery · 2016Article
- Mechanistic Asymmetry in Hsp90 Dimers.Journal of molecular biology · 2015Review
- The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Protein science : a publication of the Protein Society · 2015Review
- The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry.Oncotarget · 2015Article
- The Effect of Detergent, Temperature, and Lipid on the Oligomeric State of MscL Constructs: Insights from Mass Spectrometry.Chemistry & biology · 2015Article
- Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90.Cell reports · 2015Article
- Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Nature communications · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The Hsp90 cycle depends on the coordinated activity of a range of cochaperones, including Hop, Hsp70 and peptidyl-prolyl isomerases such as FKBP52. Using mass spectrometry, we investigate the order of addition of these cochaperones and their effects on the stoichiometry and composition of the resulting Hsp90-containing complexes. Our results show that monomeric Hop binds specifically to the Hsp90 dimer whereas FKBP52 binds to both monomeric and dimeric forms of Hsp90. By preforming Hsp90 complexes with either Hop, followed by addition of FKBP52, or with FKBP52 and subsequent addition of Hop, we monitor the formation of a predominant asymmetric ternary complex containing both cochaperones. This asymmetric complex is subsequently able to interact with the chaperone Hsp70 to form quaternary complexes containing all four proteins. Monitoring the population of these complexes during their formation and at equilibrium allows us to model the complex formation and to extract 14 different K(D) values. This simultaneous calculation of the K(D)s from a complex system with the same method, from eight deferent datasets under the same buffer conditions delivers a self-consistent set of values. In this case, the K(D) values afford insights into the assembly of ten Hsp90-containing complexes and provide a rationale for the cellular heterogeneity and prevalence of intermediates in the Hsp90 chaperone cycle.
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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.