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The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
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Hsp90 is a dimeric molecular chaperone required for the activation and stabilization of numerous client proteins many of which are involved in essential cellular processes like signal transduction pathways. This activation process is regulated by ATP-induced large conformational changes, co-chaperones and posttranslational modifications. For some co-chaperones, a detailed picture on their structures and functions exists, for others their contributions to the Hsp90 system is still unclear. Recent progress on the conformational dynamics of Hsp90 and how co-chaperones affect the Hsp90 chaperone cycle significantly increased our understanding of the gearings of this complex molecular machinery. This article is part of a Special Issue entitled: Heat Shock Protein 90 (Hsp90).
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“Hsp90 has weak intrinsic ATPase activity that is modulated by interactions with client proteins and co-chaperones.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [23]
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“The flexible Hsp90 dimer undergoes major conformational shifts during a dynamic chaperone cycle that is driven by ATP hydrolysis17,23-26 (Figure 1).”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [23]
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Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease
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“PTMs that have been documented for HSP90 and HSP70 include phosphorylation, acetylation, S-nitrosylation, oxidation, sumoylation and ubiquitination (Li et al., 2012).”
Regulatory mechanisms for amylolytic gene expression in the koji moldAspergillus oryzae
Gomi, K. (2019) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2019.1625265 · Cited by 72
“The transcription factor Mal63, the yeast counterpart of MalR, was reported to be transcriptionally activated by sequential complex formation with the chaperones Hsp70 and Hsp90 and the co-chaperone Sti1 in the presence of the inducing sugar maltose [46,47].”
BackgroundInfluentialHeat Shock Proteins and Inflammasomes
Martine, P., & Rébé, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184508 · Cited by 72
“In addition, phosphorylation, acetylation, and other post-translational modifications affect its functional state [2].”
BackgroundBhattacharya, K., & Picard, D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03962-z · Cited by 74
Mbonye, U. R., Wang, B., Gokulrangan, G., Shi, W., Yang, S., & Karn, J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001347 · Cited by 71
“ATP hydrolysis by client-bound Hsp90 leads to loss of affinity for client proteins and their release from the chaperone in a properly folded conformation (65, 67).”
BackgroundInhibiting protein-protein interactions of Hsp90 as a novel approach for targeting cancer
Gupta, S. D., Bommaka, M. K., & Banerjee, A. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.05.073 · Cited by 71
Hsp90 Inhibitors Exhibit Resistance-Free Antiviral Activity against Respiratory Syncytial Virus
Geller, R., Andino, R., & Frydman, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056762 · Cited by 71
“To achieve its role in maintaining cellular proteostasis, Hsp90 functions in concert with a large cohort of cochaperones that help regulate its activity and client specificity [12,14,32].”
BackgroundHSP 90 and co‐chaperones: a multitaskers’ view on plant hormone biology
Donato, M. D., & Geisler, M. M. (2019) · FEBS Letters · doi:10.1002/1873-3468.13499 · Cited by 66
Biaoxue, R., & Yang, S. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4214 · Cited by 66
“Co-chaperones of Hsp90 are also involved in other physiological processes, such as mitochondrial/chloroplast protein import, nuclear migration and melanoma progression (30).”
Hsp70/Hsp90 Organising Protein (Hop): Beyond Interactions with Chaperones and Prion Proteins
Baindur‐Hudson, S., Edkins, A. L., & Blatch, G. L. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-11731-7_3 · Cited by 65
Wang, T., Yu, C., Lin, Y.-S., Chen, T., Yeh, C., Liang, K., Shieh, T., Chen, C., & Hsueh, C. (2016) · Oncotarget · doi:10.18632/oncotarget.9635 · Cited by 65
“Similar to CCND1, we found that CPS1-IT1 interacts with Hsp90, a dimeric molecular chaperone that is required for the activation and stabilization of numerous proteins; many of these proteins are involved in essential cellular processes, such as signal transduction pathways [41, 42].”
BackgroundHeat shock proteins as a key defense mechanism in poultry production under heat stress conditions
Gouda, A., Tolba, S. A., Mahrose, K., Felemban, S. G., Khafaga, A. F., Khalifa, N. E., Jaremko, M., Moustafa, M., Alshaharni, M. O., Algopish, U., et al. (2024) · Poultry Science · doi:10.1016/j.psj.2024.103537 · Cited by 66
“It isn ’ t easy to overstate the importance of HSP90 chaperoning tasks connected to multiple nuclear proteins regulating DNA metabolism, repair, replication, as well as transcription and processing of RNA (Li et al. 2012).”
BackgroundInfluentialChaperone Action at the Single-Molecule Level
Mashaghi, A., Krämer, G., Lamb, D. C., Mayer, M. P., & Tans, S. J. (2013) · Chemical Reviews · doi:10.1021/cr400326k · Cited by 65
The Hsp70 chaperone is a major player in stress-induced transposable element activation
Cappucci, U., Noro, F., Casale, A. M., Fanti, L., Berloco, M. F., Alagia, A. A., Grassi, L., Pera, L. L., Piacentini, L., & Pimpinelli, S. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903936116 · Cited by 70
S100A6: molecular function and biomarker role
Wang, Y., Kang, X., Kang, X., & Yang, F. (2023) · Biomarker Research · doi:10.1186/s40364-023-00515-3 · Cited by 63
“Under adverse conditions such as stress, they can improve the resistance of cells and play a role in stress protection [76, 77].”
BackgroundA global view of Hsp90 functions
Chiosis, G., Dickey, C. A., & Johnson, J. L. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2481 · Cited by 63
Learning from Nature: Advances in Geldanamycin- and Radicicol-Based Inhibitors of Hsp90
Kitson, R. R. A., & Moody, C. J. (2013) · The Journal of Organic Chemistry · doi:10.1021/jo4002849 · Cited by 63
Biebl, M. M., Lopez, A., Rehn, A., Freiburger, L., Lawatscheck, J., Blank, B., Sattler, M., & Buchner, J. (2021) · Nature Communications · doi:10.1038/s41467-021-21063-0 · Cited by 58
Requena, J. M., Montalvo, A. M., & Fraga, J. (2015) · BioMed Research International · doi:10.1155/2015/301326 · Cited by 62
“To date, more than 20 cochaperones have been identified; they regulate the activity ofHSP90 anddetermine the interactionswith specific client proteins [10, 42].”
BackgroundContributions of Co-Chaperones and Post-Translational Modifications Towards Hsp90 Drug Sensitivity
Walton‐Diaz, A., Khan, S., Bourboulia, D., Trepel, J. B., Neckers, L., & Mollapour, M. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.88 · Cited by 59
Keep your heart in shape: molecular chaperone networks for treating heart disease
Tarone, G., & Brancaccio, M. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu049 · Cited by 61
“turnover of sarcomere proteins, required for correct contractile function and regulation of the cardiac mass.(67) Chaperone proteins can”
Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping
Rizzolo, K., Huen, J., Kumar, A., Phanse, S., Vlasblom, J., Kakihara, Y., Zeineddine, H. A., Minić, Z., Snider, J. D., Wang, W., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.074 · Cited by 64
Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis
Honoré, F. A., Méjean, V., & Genest, O. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.082 · Cited by 59
“Hsp90 is a highly dynamic protein (Flynn et al., 2015; Krukenberg et al., 2011; Li et al., 2012; Mayer and Le Breton, 2015; Shiau et al., 2006) with several conformations that are influenced by the presence of nucleotides (ATP or ADP) bound to the N-domain.”
BackgroundMultifaceted roles of HEAT SHOCK PROTEIN 90 molecular chaperones in plant development
Tichá, T., Samakovli, D., Kuchařová, A., Vavrdová, T., & Šamaj, J. (2020) · Journal of Experimental Botany · doi:10.1093/jxb/eraa177 · Cited by 60
Song, D., Li, L.-S., Heaton-Johnson, K. J., Arsenault, P. R., Master, S. R., & Lee, F. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.440552 · Cited by 59
“HSP90 can associate with a multitude of co-chaperones that perform a number of functions, including the recruitment of regulatory or client proteins to the HSP90 machinery (23, 25, 26).”
BackgroundHsp90@chromatin.nucleus: an emerging hub of a networker
Sawarkar, R., & Paro, R. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.11.007 · Cited by 55
Prince, T. L., Kijima, T., Tatokoro, M., Lee, S., Tsutsumi, S., Yim, K. H., Rivas, C., Alarcon, S. V., Schwartz, H., Khamit-Kush, K. K., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141786 · Cited by 57
“The molecular chaperone heat shock protein 90 (HSP90) has been conserved throughout evolution, and functions primarily by coupling ATP hydrolysis to a cycle of structural rearrangements that drives the binding, folding and release of client proteins (Fig 1A) [1] [2].”
BackgroundHigh-Resolution Structural Analysis Shows How Tah1 Tethers Hsp90 to the R2TP Complex
Back, R., Dominguez, C., Rothé, B., Bobo, C., Beaufils, C., Moréra, S., Meyer, P., Charpentier, B., Branlant, C., Allain, F. H. ‐., et al. (2013) · Structure · doi:10.1016/j.str.2013.07.024 · Cited by 56
Shigeta, T., Zaizen, Y., Sugimoto, Y., Nakamura, Y. K., Matsuo, T., & Okamoto, S. (2015) · Journal of Plant Physiology · doi:10.1016/j.jplph.2015.02.003 · Cited by 54
“…i o o t s M P p b 1 T S C p B h M I s w e T I H o d w u J f E 0 T. Shigeta et al. / Journal of P roteins to fulfill diverse functions in eukaryotes (Li et al., 2012). o date, HSP90 proteins have been identified from different plant pecies, some of which have been shown to play important roles in…”
BackgroundChen, X., Liu, P., Wang, Q., Li, Y., Li, F., Fu, H., Zhu, J., Chen, Z., Zhu, W., Xie, C., et al. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.07.012 · Cited by 55
Metadata
- Authors
- Li, J., Soroka, J., & Buchner, J.
- Affiliations
- Technical University of Munich (DE)
- Center for Integrated Protein Science Munich (DE)
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 1823
- Issue
- 3
- Pages
- 624-635
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2093169681
- Cited by
- 498
- References
- 217
- Citations by year
- 2026: 7 · 2025: 18 · 2024: 15 · 2023: 23 · 2022: 31 · 2021: 39 · 2020: 45 · 2019: 44 · 2018: 54 · 2017: 39 · 2016: 51 · 2015: 35 · 2014: 45 · 2013: 33 · 2012: 15
- FWCI
- 2.76
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- HSP90, molecular chaperones, co-chaperones, conformational dynamics, ATP-induced conformational change, chaperone cycle, post-translational modification, signal transduction
- MeSH terms
- Adenosine Triphosphate, Animals, Binding Sites, Humans, Models, Molecular, Protein Binding, Protein Conformation, Molecular Chaperones, HSP90 Heat-Shock Proteins
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