Cited by 504Heat shock proteins researchProtein Structure and DynamicsUbiquitin and proteasome pathways

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The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

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Li, Jing, Soroka, Joanna, Buchner, Johannes·2012·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

DOI 10.1016/j.bbamcr.2011.09.003

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Abstract

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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Additional file 2 of Curcumin derivative C212 inhibits Hsp90 and eliminates both growing and quiescent leukemia cells in deep dormancy
Liu, B., Shen, Y., Huang, H., Croce, K. D., Wu, M., Fan, Y., Liu, Y., Xu, J., & Yao, G. (2020) · Figshare · doi:10.6084/m9.figshare.13024455
Additional file 2 of The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation
Chang, Y.-L., Yang, C.-C., Huang, Y.-Y., Chen, Y.-A., Yang, C.-W., Liao, C.-Y., Li, H., Wu, C.-S., Lin, C.-H., & Teng, S.-C. (2024) · Figshare · doi:10.6084/m9.figshare.24864323
Additional file 5 of An HSP90 cochaperone Ids2 maintains the stability of mitochondrial DNA and ATP synthase
Jiang, P.-H., Hou, C.-Y., & Teng, S.-C. (2021) · Figshare · doi:10.6084/m9.figshare.16994450
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Regulation of proteotoxicity through atypical NEDDylation
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Amoah, D. P., Bhat, R. K., Trad, M., Hussein, S. K., Overduin, M., & LaPointe, P. (2026) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2026.100179
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Adedeji, A., Unruh, E., Derr, A., Ndolo, C., Balch, M., Paul, K., Morton, A. J., & Kravats, A. N. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113358
“Hsp90 is widely recognized as a classical “holdase”, functioning in stabilizing unfolded polypeptides and preventing protein aggregation (9, 48, 61–63).”
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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)
DOI: 10.1016/j.bbamcr.2011.09.003
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 504 d)
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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The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

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