ArticleNature communications2023
Nucleotide exchange is sufficient for Hsp90 functions in vivo.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- 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
- Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome.Cell stress & chaperones · 2026Article
- The GHKL ATPase Family as a Paradigm for MutL Homolog Function in DNA Mismatch Repair.International journal of molecular sciences · 2025Review
- Collaboration between two conserved sequence motifs drives ATPase stimulation of Hsp90 by Aha1.Protein science : a publication of the Protein Society · 2025Article
- ATP plays a structural role in Hsp90 function.Nature communications · 2025Article
- Hsp90: Bringing it all together.Cell stress & chaperones · 2025Review
- 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
- Dominant negative mutations in yeast Hsp90 indicate triage decision mechanism targeting client proteins for degradation.Molecular biology of the cell · 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
- Recruitment of Ahsa1 to Hsp90 is regulated by a conserved peptide that inhibits ATPase stimulation.EMBO reports · 2024Article
- 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
- The role of Aha1 in cancer and neurodegeneration.Frontiers in molecular neuroscience · 2024Review
- Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Hsp90 is an essential eukaryotic chaperone that regulates the activity of many client proteins. Current models of Hsp90 function, which include many conformational rearrangements, specify a requirement of ATP hydrolysis. Here we confirm earlier findings that the Hsp82-E33A mutant, which binds ATP but does not hydrolyze it, supports viability of S. cerevisiae, although it displays conditional phenotypes. We find binding of ATP to Hsp82-E33A induces the conformational dynamics needed for Hsp90 function. Hsp90 orthologs with the analogous EA mutation from several eukaryotic species, including humans and disease organisms, support viability of both S. cerevisiae and Sz. pombe. We identify second-site suppressors of EA that rescue its conditional defects and allow EA versions of all Hsp90 orthologs tested to support nearly normal growth of both organisms, without restoring ATP hydrolysis. Thus, the requirement of ATP for Hsp90 to maintain viability of evolutionarily distant eukaryotic organisms does not appear to depend on energy from ATP hydrolysis. Our findings support earlier suggestions that exchange of ATP for ADP is critical for Hsp90 function. ATP hydrolysis is not necessary for this exchange but provides an important control point in the cycle responsive to regulation by co-chaperones.
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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.