The known unknowns of the Hsp90 chaperone
Molecular chaperones are vital proteins that maintain protein homeostasis by assisting in protein folding, activation, degradation, and stress protection. Among them, heat-shock protein 90 (Hsp90) stands out as an essential proteostasis hub in eukaryotes, chaperoning hundreds of ‘clients’ (substrate...
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2024-12-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/102666 |
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| author | Laura-Marie Silbermann Benjamin Vermeer Sonja Schmid Katarzyna Tych |
| author_facet | Laura-Marie Silbermann Benjamin Vermeer Sonja Schmid Katarzyna Tych |
| author_sort | Laura-Marie Silbermann |
| collection | DOAJ |
| description | Molecular chaperones are vital proteins that maintain protein homeostasis by assisting in protein folding, activation, degradation, and stress protection. Among them, heat-shock protein 90 (Hsp90) stands out as an essential proteostasis hub in eukaryotes, chaperoning hundreds of ‘clients’ (substrates). After decades of research, several ‘known unknowns’ about the molecular function of Hsp90 remain unanswered, hampering rational drug design for the treatment of cancers, neurodegenerative, and other diseases. We highlight three fundamental open questions, reviewing the current state of the field for each, and discuss new opportunities, including single-molecule technologies, to answer the known unknowns of the Hsp90 chaperone. |
| format | Article |
| id | doaj-art-ec8800e8d6974114b03f729cfad3a9c3 |
| institution | Kabale University |
| issn | 2050-084X |
| language | English |
| publishDate | 2024-12-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj-art-ec8800e8d6974114b03f729cfad3a9c32025-01-28T11:57:07ZengeLife Sciences Publications LtdeLife2050-084X2024-12-011310.7554/eLife.102666The known unknowns of the Hsp90 chaperoneLaura-Marie Silbermann0https://orcid.org/0000-0001-5989-1774Benjamin Vermeer1https://orcid.org/0000-0002-8375-2966Sonja Schmid2https://orcid.org/0000-0002-3710-5602Katarzyna Tych3https://orcid.org/0000-0001-9091-0507Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, NetherlandsLaboratory of Biophysics, Wageningen University & Research, Wageningen, NetherlandsLaboratory of Biophysics, Wageningen University & Research, Wageningen, NetherlandsGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, NetherlandsMolecular chaperones are vital proteins that maintain protein homeostasis by assisting in protein folding, activation, degradation, and stress protection. Among them, heat-shock protein 90 (Hsp90) stands out as an essential proteostasis hub in eukaryotes, chaperoning hundreds of ‘clients’ (substrates). After decades of research, several ‘known unknowns’ about the molecular function of Hsp90 remain unanswered, hampering rational drug design for the treatment of cancers, neurodegenerative, and other diseases. We highlight three fundamental open questions, reviewing the current state of the field for each, and discuss new opportunities, including single-molecule technologies, to answer the known unknowns of the Hsp90 chaperone.https://elifesciences.org/articles/102666Hsp90molecular chaperonesproteostasis |
| spellingShingle | Laura-Marie Silbermann Benjamin Vermeer Sonja Schmid Katarzyna Tych The known unknowns of the Hsp90 chaperone eLife Hsp90 molecular chaperones proteostasis |
| title | The known unknowns of the Hsp90 chaperone |
| title_full | The known unknowns of the Hsp90 chaperone |
| title_fullStr | The known unknowns of the Hsp90 chaperone |
| title_full_unstemmed | The known unknowns of the Hsp90 chaperone |
| title_short | The known unknowns of the Hsp90 chaperone |
| title_sort | known unknowns of the hsp90 chaperone |
| topic | Hsp90 molecular chaperones proteostasis |
| url | https://elifesciences.org/articles/102666 |
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