ArticleNature chemical biology2016
Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism.
Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Post‑translational modifications in atherosclerosis: Roles, mechanisms and therapeutic potential (Review).International journal of molecular medicine · 2026Review
- Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation.Nature communications · 2026Article
- Nucleotide-dependent domain interactions of Aha1-type co-chaperones with Hsp90 reveal evolutionarily conserved binding determinants.Cell stress & chaperones · 2026Review
- Beyond Folding: Expanding the Functional Landscape of Hsp90 Chaperone Machinery in Health and Disease.International journal of molecular sciences · 2025Review
- Nitration-driven structural changes in Hsp90 linked to gain of pathological functions.The Biochemical journal · 2025Article
- ATP plays a structural role in Hsp90 function.Nature communications · 2025Article
- Ordered ATP hydrolysis in the Hsp90 chaperone is regulated by Aha1 and a conserved post-translational modification.Protein science : a publication of the Protein Society · 2025Article
- The known unknowns of the Hsp90 chaperone.eLife · 2024Review
- The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding.Nature communications · 2024Article
- Establishing Order Through Disorder by the Hsp90 Molecular Chaperone.Journal of molecular biology · 2024Review
- Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024Review
- Structural transitions modulate the chaperone activities of Grp94.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90.Nature communications · 2024Article
- Unveiling the orchestration: mycobacterial small RNAs as key mediators in host-pathogen interactions.Frontiers in microbiology · 2024Review
- The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Domain swap facilitates structural transitions of spider silk protein C-terminal domains.Protein science : a publication of the Protein Society · 2023Article
- Prediction model of stress ulcer after laparoscopic surgery for colorectal cancer established by machine learning algorithm.World journal of gastrointestinal surgery · 2023Article
- Aha1 regulates Hsp90's conformation and function in a stoichiometry-dependent way.Biophysical journal · 2023Article
- Nucleotide exchange is sufficient for Hsp90 functions in vivo.Nature communications · 2023Article
- Visualizing the transiently populated closed-state of human HSP90 ATP binding domain.Nature communications · 2022Article
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7 authors.
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Abstract
The Hsp90 chaperone is a central node of protein homeostasis, activating many diverse client proteins. Hsp90 functions as a molecular clamp that closes and opens in response to the binding and hydrolysis of ATP. Crystallographic studies have defined distinct conformational states of the mechanistic core, implying structural changes that have not yet been observed in solution. Here we engineered one-nanometer fluorescence probes based on photoinduced electron transfer into the yeast Hsp90 to observe these motions. We found that the ATPase activity of the chaperone was reflected in the kinetics of specific structural rearrangements at remote positions that acted cooperatively. Nanosecond single-molecule fluorescence fluctuation analysis uncovered that critical structural elements that undergo rearrangement were mobile on a sub-millisecond time scale. We identified a two-step mechanism for lid closure over the nucleotide-binding pocket. The activating co-chaperone Aha1 mobilized the lid of apo Hsp90, suggesting an early role in the catalytic cycle.
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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.