Hsp90 Chaperone in Disease

S.G.D. Rüdiger; L. Ferrari

doi:10.1007/978-3-030-23158-3_21

Hsp90 Chaperone in Disease

S.G.D. Rüdiger
, L. Ferrari

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic › peer-review

Abstract

The molecular chaperone Hsp90 is at the heart of protein homeostasis control. A wide range of pathologies disturbs protein homeostasis, thus placing Hsp90 at the crossroads of many diseases. Here, we evaluate the impact of recent progress in understanding the molecular mechanism of Hsp90-client interactions and their role in disease. We discuss the role of Hsp90 for hormonal imbalances, cancer and neurodegenerative disorders. For each disease class we discuss implications of complexes in which Hsp90 binds to a paradigmatic client: the transcription factor Glucocorticoid Receptor, the kinase Cdk4 and the microtubule stabilizer Tau. The mechanistic insights allow us to elaborate on possible therapeutic intervention routes. Hsp90 is a druggable chaperone. Thus, understanding Hsp90 biology at molecular resolution offers an interesting approach to tackle protein-related diseases.

Original language	English
Title of host publication	Heat Shock Protein 90 in Human Diseases and Disorders
Editors	Alexzander A. A. Asea, Punit Kaur
Publisher	Springer
Pages	473-491
Edition	1
ISBN (Electronic)	978-3-030-23158-3
ISBN (Print)	978-3-030-23157-6, 978-3-030-23160-6
DOIs	https://doi.org/10.1007/978-3-030-23158-3_21
Publication status	Published - 15 Nov 2019

Publication series

Name	Heat Shock Proteins
Publisher	Springer
Volume	19
ISSN (Print)	1877-1246
ISSN (Electronic)	1877-1254

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Kinases
Molecular chaperones
Neurodegeneration
Protein folding
Proteostasis
Steroid receptors
ad

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10.1007/978-3-030-23158-3_21

Ferrari-Rüdiger2019_Chapter_Hsp90ChaperoneInDiseaseFinal published version, 651 KBLicence: Taverne

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KW - Molecular chaperones

KW - Neurodegeneration

KW - Protein folding

KW - Proteostasis

KW - Steroid receptors

KW - ad

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Hsp90 Chaperone in Disease

Abstract

Publication series

UN SDGs

Keywords

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