Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

LAUR Repository

Show simple item record

dc.contributor.author Akoury, Elias
dc.contributor.author Duarte, Afonso M.S.
dc.contributor.author Didenko, Tatiana
dc.contributor.author Radil, Martina
dc.date.accessioned 2019-03-21T14:18:56Z
dc.date.available 2019-03-21T14:18:56Z
dc.date.copyright 2014 en_US
dc.date.issued 2019-03-21
dc.identifier.issn 1097-4172 en_US
dc.identifier.uri http://hdl.handle.net/10725/10247
dc.description.abstract 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. en_US
dc.language.iso en en_US
dc.title Hsp90-Tau complex reveals molecular basis for specificity in chaperone action en_US
dc.type Article en_US
dc.description.version Published en_US
dc.author.school SAS en_US
dc.author.idnumber 201900590 en_US
dc.author.department Natural Sciences en_US
dc.description.embargo N/A en_US
dc.relation.journal Cell en_US
dc.journal.volume 156 en_US
dc.journal.issue 5 en_US
dc.article.pages 963-974 en_US
dc.identifier.doi https://doi.org/10.1016/j.cell.2014.01.037 en_US
dc.identifier.ctation 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. en_US
dc.author.email elias.akoury@lau.edu.lb en_US
dc.identifier.tou http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php en_US
dc.identifier.url https://www.sciencedirect.com/science/article/pii/S0092867414000890#! en_US
dc.orcid.id https://orcid.org/0000-0001-5202-8935 en_US
dc.author.affiliation Lebanese American University en_US

Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record

Search LAUR

Advanced Search


My Account