ArticleGenetics2012
Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae.
Article in Genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Advances in the structures, mechanisms and targeting of molecular chaperones.Signal transduction and targeted therapy · 2025Review
- Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function.PLoS genetics · 2024Article
- Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function.Essays in biochemistry · 2023Article
- Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle.PLoS genetics · 2023Article
- Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.Genetics · 2021Article
- Does Inter-Organellar Proteostasis Impact Yeast Quality and Performance During Beer Fermentation?Frontiers in genetics · 2020Article
- Structure, Function, and Regulation of the Hsp90 Machinery.Cold Spring Harbor perspectives in biology · 2019Review
- Article
- Hsp90 inhibition renders iNOS aggregation and the clearance of iNOS aggregates by proteasomes requires SPSB2.Free radical biology & medicine · 2018Article
- The HSP90 chaperone machinery.Nature reviews. Molecular cell biology · 2017Review
- An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.Nature communications · 2017Article
- Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.PLoS genetics · 2015Article
- The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome.Eukaryotic cell · 2015Article
- The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.Current genetics · 2014Article
- The ribosomal biogenesis protein Utp21 interacts with Hsp90 and has differing requirements for Hsp90-associated proteins.PloS one · 2014Article
- Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis.The Journal of biological chemistry · 2013Article
- Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.Future medicinal chemistry · 2013Review
- Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.Nature structural & molecular biology · 2013Article
- Identification of chaperones in freeze tolerance in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock protein 90 (Hsp90) of Saccharomyces cerevisiae is an abundant essential eukaryotic molecular chaperone involved in the activation and stabilization of client proteins, including several transcription factors and oncogenic kinases. Hsp90 undergoes a complex series of conformational changes and interacts with partner co-chaperones such as Sba1, Cpr6, Cpr7, and Cns1 as it binds and hydrolyzes ATP. In the absence of nucleotide, Hsp90 is dimerized only at the carboxy-terminus. In the presence of ATP, Hsp90 also dimerizes at the amino-terminus, creating a binding site for Sba1. Truncation of a charged linker region of yeast Hsp90 (Hsp82Δlinker) was known to disrupt the ability of Hsp82 to undergo amino-terminal dimerization and bind Sba1. We found that yeast expressing Hsp82Δlinker constructs exhibited a specific synthetic lethal phenotype in cells lacking CPR7. The isolated tetratricopeptide repeat domain of Cpr7 was both necessary and sufficient for growth in those strains. Cpr6 and Cpr7 stably bound the carboxy-terminus of wild-type Hsp82 only in the presence of nonhydrolyzable ATP and formed an Hsp82-Cpr6-Cpr7 ternary complex. However, in cells expressing Hsp82Δlinker or lacking CPR7, Cpr6 was able to bind Hsp82 in the presence or absence of nucleotide. Overexpression of CNS1, but not of other co-chaperones, in cpr7 cells restored nucleotide-dependent Hsp82-Cpr6 interaction. Together, our results suggest that the in vivo functions of Cpr7 include modulating Hsp90 conformational changes, mediating proper signaling of the nucleotide-bound state to the carboxy-terminus of Hsp82, or regulating Hsp82-Cpr6 interaction.
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