Zhao, R. et al. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the Hsp90 chaperone. Cell 120, 715–727 (2005).
Article CAS PubMed Google Scholar
Taipale, M., Jarosz, D. F. & Lindquist, S. Hsp90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 11, 515–528 (2010).
Article CAS PubMed Google Scholar
Taipale, M. et al. Quantitative analysis of Hsp90–client interactions reveals principles of substrate recognition. Cell 150, 987–1001 (2012).
Article CAS PubMed PubMed Central Google Scholar
Lackie, R. E. et al. The Hsp70/Hsp90 chaperone machinery in neurodegenerative diseases. Front Neurosci. 11, 254 (2017).
Article PubMed PubMed Central Google Scholar
Kolhe, J. A., Babu, N. L. & Freeman, B. C. The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions. Mol. Cell 83, 2035–2044 (2023).
Article CAS PubMed Google Scholar
Whitesell, L. & Lindquist, S. L. Hsp90 and the chaperoning of cancer. Nat. Rev. Cancer 5, 761–772 (2005).
Article CAS PubMed Google Scholar
Trepel, J., Mollapour, M., Giaccone, G. & Neckers, L. Targeting the dynamic Hsp90 complex in cancer. Nat. Rev. Cancer 10, 537–549 (2010).
Article CAS PubMed PubMed Central Google Scholar
Jaeger, A. M. & Whitesell, L. Hsp90: enabler of cancer adaptation. Annu. Rev. Cancer Biol. 3, 275–297 (2019).
Shiau, A. K., Harris, S. F., Southworth, D. R. & Agard, D. A. Structural analysis of E. coli Hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 127, 329–340 (2006).
Article CAS PubMed Google Scholar
Wickner, S., Nguyen, T. L. & Genest, O. The bacterial Hsp90 chaperone: cellular functions and mechanism of action. Annu Rev. Microbiol 75, 719–739 (2021).
Article CAS PubMed Google Scholar
Krukenberg, K. A., Forster, F., Rice, L. M., Sali, A. & Agard, D. A. Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure 16, 755–765 (2008).
Article CAS PubMed PubMed Central Google Scholar
Southworth, D. R. & Agard, D. A. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Mol. Cell 32, 631–640 (2008).
Article CAS PubMed PubMed Central Google Scholar
Ali, M. M. et al. Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex. Nature 440, 1013–1017 (2006).
Article CAS PubMed PubMed Central Google Scholar
Kirschke, E., Goswami, D., Southworth, D., Griffin, P. R. & Agard, D. A. Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles. Cell 157, 1685–1697 (2014).
Article CAS PubMed PubMed Central Google Scholar
Verba, K. A. et al. Atomic structure of Hsp90–Cdc37–Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. Science 352, 1542–1547 (2016).
Article CAS PubMed PubMed Central Google Scholar
Wang, R. Y. et al. Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism. Nature 601, 460–464 (2022).
Article CAS PubMed Google Scholar
Noddings, C. M., Wang, R. Y., Johnson, J. L. & Agard, D. A. Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism. Nature 601, 465–469 (2022).
Article CAS PubMed Google Scholar
Hellenkamp, B., Wortmann, P., Kandzia, F., Zacharias, M. & Hugel, T. Multidomain structure and correlated dynamics determined by self-consistent FRET networks. Nat. Methods 14, 174–180 (2017).
Article CAS PubMed Google Scholar
Mickler, M., Hessling, M., Ratzke, C., Buchner, J. & Hugel, T. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat. Struct. Mol. Biol. 16, 281–286 (2009).
Article CAS PubMed Google Scholar
Saio, T., Guan, X., Rossi, P., Economou, A. & Kalodimos, C. G. Structural basis for protein antiaggregation activity of the trigger factor chaperone. Science 344, 1250494 (2014).
Article PubMed PubMed Central Google Scholar
Karagoz, G. E. et al. Hsp90–tau complex reveals molecular basis for specificity in chaperone action. Cell 156, 963–974 (2014).
Article PubMed PubMed Central Google Scholar
Huang, C., Rossi, P., Saio, T. & Kalodimos, C. G. Structural basis for the antifolding activity of a molecular chaperone. Nature 537, 202–206 (2016).
Article CAS PubMed PubMed Central Google Scholar
Huang, C. & Kalodimos, C. G. Structures of large protein complexes determined by nuclear magnetic resonance spectroscopy. Annu. Rev. Biophys. 46, 317–336 (2017).
Article CAS PubMed Google Scholar
Jiang, Y., Rossi, P. & Kalodimos, C. G. Structural basis for client recognition and activity of Hsp40 chaperones. Science 365, 1313–1319 (2019).
Article CAS PubMed PubMed Central Google Scholar
Rosenzweig, R. & Kay, L. E. Bringing dynamic molecular machines into focus by methyl-TROSY NMR. Annu. Rev. Biochem. 83, 291–315 (2014).
Article CAS PubMed Google Scholar
Burmann, B. M. et al. Regulation of α-synuclein by chaperones in mammalian cells. Nature 577, 127–132 (2020).
Article CAS PubMed Google Scholar
Faust, O. et al. Hsp40 proteins use class-specific regulation to drive Hsp70 functional diversity. Nature 587, 489–494 (2020).
Article CAS PubMed Google Scholar
Street, T. O., Lavery, L. A. & Agard, D. A. Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Mol. Cell 42, 96–105 (2011).
Article CAS PubMed PubMed Central Google Scholar
Balasubramanian, A., Markovski, M., Hoskins, J. R., Doyle, S. M. & Wickner, S. Hsp90 of E. coli modulates assembly of FtsZ, the bacterial tubulin homolog. Proc. Natl Acad. Sci. USA 116, 12285–12294 (2019).
Article CAS PubMed PubMed Central Google Scholar
Takeuchi, K. & Wagner, G. NMR studies of protein interactions. Curr. Opin. Struct. Biol. 16, 109–117 (2006).
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