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Structure, Function, and Regulation of the Hsp90 Machinery

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Biebl, Maximilian M., Buchner, Johannes·2019·Cold Spring Harbor Perspectives in Biology

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Abstract

Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a plethora of substrates ("clients"), including protein kinases, transcription factors, and E3 ubiquitin ligases, positioning Hsp90 as a central regulator of cellular proteostasis. Hsp90 undergoes large conformational changes during its ATPase cycle. The processing of clients by cytosolic Hsp90 is assisted by a cohort of cochaperones that affect client recruitment, Hsp90 ATPase function or conformational rearrangements in Hsp90. Because of the importance of Hsp90 in regulating central cellular pathways, strategies for the pharmacological inhibition of the Hsp90 machinery in diseases such as cancer and neurodegeneration are being developed. In this review, we summarize recent structural and mechanistic progress in defining the function of organelle-specific and cytosolic Hsp90, including the impact of individual cochaperones on the maturation of specific clients and complexes with clients as well as ways of exploiting Hsp90 as a drug target.

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The Chloroplast DnaJ Homolog CDJ1 of Chlamydomonas reinhardtii Is Part of a Multichaperone Complex Containing HSP70B, CGE1, and HSP90C
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Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide
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Chaperone ligand-discrimination by the TPR-domain protein Tah1
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Regulation of the Hsp90 system
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Functional Interactions between Hsp90 and the Co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae
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The Peptidyl-prolyl Isomerase Domain of the CyP-40 Cyclophilin Homolog Cpr7 Is Not Required to Support Growth or Glucocorticoid Receptor Activity in Saccharomyces cerevisiae
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Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate
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“Most recently, a substance specifically disrupting the Hsp90:GR: FKBP51 complex was found, which did not impede the binding of FKPB52 to Hsp90 (Sabbagh et al. 2018).”
Background
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A chemical compound inhibiting the Aha1–Hsp90 chaperone complex
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Designed Hsp90 Heterodimers Reveal an Asymmetric ATPase-Driven Mechanism In Vivo
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The FKBP5 polymorphism rs1360780 influences the effect of an algorithm-based antidepressant treatment and is associated with remission in patients with major depression
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STA-8666, a novel HSP90 inhibitor/SN-38 drug conjugate, causes complete tumor regression in preclinical mouse models of pediatric sarcoma
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The common functional FKBP5 variant rs1360780 is associated with altered cognitive function in aged individuals
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Cdc37 (Cell Division Cycle 37) Restricts Hsp90 (Heat Shock Protein 90) Motility by Interaction with N-terminal and Middle Domain Binding Sites
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Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites
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An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
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A switch point in the molecular chaperone Hsp90 responding to client interaction
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Chaperoning the Chaperone: A Role for the Co-chaperone Cpr7 in Modulating Hsp90 Function in Saccharomyces cerevisiae
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HSP90 Inhibitor–SN-38 Conjugate Strategy for Targeted Delivery of Topoisomerase I Inhibitor to Tumors
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Hsp90 invades the outside
Picard, D. (2004) · Nature Cell Biology · doi:10.1038/ncb0604-479 · Cited by 34
Past, present, and emerging roles of mitochondrial heat shock protein TRAP1 in the metabolism and regulation of cancer stem cells
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Hsf1 Phosphorylation Generates Cell-to-Cell Variation in Hsp90 Levels and Promotes Phenotypic Plasticity
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Role of HSP90 in the Regulation of de Novo Purine Biosynthesis
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Reconstructing the Hsp90/Tau Machine
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Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism
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The Hsp90 Cochaperones Cpr6, Cpr7, and Cns1 Interact with the Intact Ribosome
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Characterization of an Hsp90-Independent Interaction between Co-Chaperone p23 and Transcription Factor p53
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See all 304

Authors: Biebl, M. M., & Buchner, J.
Venue: Cold Spring Harbor Perspectives in Biology
Publisher: Cold Spring Harbor Laboratory
Published: 2019-02-11
Volume: 11
Issue: 9
Pages: a034017
ISSN: 1943-0264 (ISSN-L)
DOI: 10.1101/cshperspect.a034017
OpenAlex: W2913172834
Cited by: 304
References: 322
Type: posted content
Language: en
Open access: bronze

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Structure, Function, and Regulation of the Hsp90 Machinery

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