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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Marozkina, N. V., Yemen, S., Borowitz, M., Liu, L., Plapp, M., Sun, F., Islam, R. M., Erdmann-Gilmore, P., Townsend, R. R., Lichti, C. F., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909128107 · Cited by 72
Hsp90 Is Essential for Restoring Cellular Functions of Temperature-sensitive p53 Mutant Protein but Not for Stabilization and Activation of Wild-type p53
Müller, P., Češková, P., & Vojtesek, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412767200 · Cited by 69
Structural and functional analysis of SGT1–HSP90 core complex required for innate immunity in plants
Kadota, Y., Amigues, B., Ducassou, L., Madaoui, H., Ochsenbein, F., Guérois, R., & Shirasu, K. (2008) · EMBO Reports · doi:10.1038/embor.2008.185 · Cited by 68
Heat shock protein 90 facilitates formation of the HBV capsid via interacting with the HBV core protein dimers
Shim, H. Y., Quan, X., Yi, Y., & Jung, G. (2010) · Virology · doi:10.1016/j.virol.2010.11.005 · Cited by 67
Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity
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Hsp90 increases LIM kinase activity by promoting its homo‐dimerization
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Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen
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P59 (FK506 binding protein 59) interaction with heat shock proteins is highly conserved and may involve proteins other than steroid receptors
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Molecular Chaperone Functions in Protein Folding and Proteostasis
Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,545
In vivo aspects of protein folding and quality control
Balchin, D., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,477
“p23 acts toward the end of the cycle, and facilitates client maturation by stabilizing the closed state of the Hsp90 N domains and inhibiting ATP hydrolysis (107).”
Background
Chaperone machines for protein folding, unfolding and disaggregation
Saibil, H. R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3658 · Cited by 1,211
Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials
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“which regulate the cancer cell’s growth and apoptosis signaling pathways.(105,106) Hsp90 stabilizes the conformation of the client proteins mentioned above and prevents them from ubiquitination-mediated degradation, thereby stabilizes them to stay in the active form and promotes the tumor growth and metastasis (Fig.”
Background
The heat‐shock protein/chaperone network and multiple stress resistance
Jacob, P., Hirt, H., & Bendahmane, A. (2016) · Plant Biotechnology Journal · doi:10.1111/pbi.12659 · Cited by 776
“Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd., 15, 405–414 immunity, as HSP70 and HSP90 often cooperate in large multichaperone complexes (Li et al., 2012).”
Background

See all 504

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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