Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly because the substrate specificity of Hsp90 is poo...
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| المؤلف الرئيسي: | |
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| مؤلفون آخرون: | , , |
| التنسيق: | article |
| منشور في: |
2014
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| الوصول للمادة أونلاين: | http://hdl.handle.net/10725/10247 https://doi.org/10.1016/j.cell.2014.01.037 http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php https://www.sciencedirect.com/science/article/pii/S0092867414000890#! |
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| _version_ | 1864513486219902976 |
|---|---|
| author | Akoury, Elias |
| author2 | Duarte, Afonso M.S. Didenko, Tatiana Radil, Martina |
| author2_role | author author author |
| author_facet | Akoury, Elias Duarte, Afonso M.S. Didenko, Tatiana Radil, Martina |
| author_role | author |
| dc.creator.none.fl_str_mv | Akoury, Elias Duarte, Afonso M.S. Didenko, Tatiana Radil, Martina |
| dc.date.none.fl_str_mv | 2014 2019-03-21T14:18:56Z 2019-03-21T14:18:56Z 2019-03-21 |
| dc.identifier.none.fl_str_mv | 1097-4172 http://hdl.handle.net/10725/10247 https://doi.org/10.1016/j.cell.2014.01.037 Karagöz, G. E., Duarte, A. M., Akoury, E., Ippel, H., Biernat, J., Luengo, T. M., ... & Dickey, C. A. (2014). Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell, 156(5), 963-974. http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php https://www.sciencedirect.com/science/article/pii/S0092867414000890#! |
| dc.language.none.fl_str_mv | en |
| dc.relation.none.fl_str_mv | Cell |
| dc.rights.*.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.title.none.fl_str_mv | Hsp90-Tau complex reveals molecular basis for specificity in chaperone action |
| dc.type.none.fl_str_mv | Article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
| description | Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly because the substrate specificity of Hsp90 is poorly understood. Here, we obtained a structural model of Hsp90 in complex with its natural disease-associated substrate, the intrinsically disordered Tau protein. Hsp90 binds to a broad region in Tau that includes the aggregation-prone repeats. Complementarily, a 106-Å-long substrate-binding interface in Hsp90 enables many low-affinity contacts. This allows recognition of scattered hydrophobic residues in late folding intermediates that remain after early burial of the Hsp70 sites. Our model resolves the paradox of how Hsp90 specifically selects for late folding intermediates but also for some intrinsically disordered proteins—through the eyes of Hsp90 they look the same. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | LAURepo_9f37bafae531b456911086a9eaa4d770 |
| identifier_str_mv | 1097-4172 Karagöz, G. E., Duarte, A. M., Akoury, E., Ippel, H., Biernat, J., Luengo, T. M., ... & Dickey, C. A. (2014). Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell, 156(5), 963-974. |
| language_invalid_str_mv | en |
| network_acronym_str | LAURepo |
| network_name_str | Lebanese American University repository |
| oai_identifier_str | oai:laur.lau.edu.lb:10725/10247 |
| publishDate | 2014 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| spelling | Hsp90-Tau complex reveals molecular basis for specificity in chaperone actionAkoury, EliasDuarte, Afonso M.S.Didenko, TatianaRadil, MartinaProtein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly because the substrate specificity of Hsp90 is poorly understood. Here, we obtained a structural model of Hsp90 in complex with its natural disease-associated substrate, the intrinsically disordered Tau protein. Hsp90 binds to a broad region in Tau that includes the aggregation-prone repeats. Complementarily, a 106-Å-long substrate-binding interface in Hsp90 enables many low-affinity contacts. This allows recognition of scattered hydrophobic residues in late folding intermediates that remain after early burial of the Hsp70 sites. Our model resolves the paradox of how Hsp90 specifically selects for late folding intermediates but also for some intrinsically disordered proteins—through the eyes of Hsp90 they look the same.PublishedN/A2019-03-21T14:18:56Z2019-03-21T14:18:56Z20142019-03-21Articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1097-4172http://hdl.handle.net/10725/10247https://doi.org/10.1016/j.cell.2014.01.037Karagöz, G. E., Duarte, A. M., Akoury, E., Ippel, H., Biernat, J., Luengo, T. M., ... & Dickey, C. A. (2014). Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell, 156(5), 963-974.http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.phphttps://www.sciencedirect.com/science/article/pii/S0092867414000890#!enCellinfo:eu-repo/semantics/openAccessoai:laur.lau.edu.lb:10725/102472021-03-19T10:45:22Z |
| spellingShingle | Hsp90-Tau complex reveals molecular basis for specificity in chaperone action Akoury, Elias |
| status_str | publishedVersion |
| title | Hsp90-Tau complex reveals molecular basis for specificity in chaperone action |
| title_full | Hsp90-Tau complex reveals molecular basis for specificity in chaperone action |
| title_fullStr | Hsp90-Tau complex reveals molecular basis for specificity in chaperone action |
| title_full_unstemmed | Hsp90-Tau complex reveals molecular basis for specificity in chaperone action |
| title_short | Hsp90-Tau complex reveals molecular basis for specificity in chaperone action |
| title_sort | Hsp90-Tau complex reveals molecular basis for specificity in chaperone action |
| url | http://hdl.handle.net/10725/10247 https://doi.org/10.1016/j.cell.2014.01.037 http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php https://www.sciencedirect.com/science/article/pii/S0092867414000890#! |