Hsp90: From Cellular to Organismal Proteostasis

Milán Somogyvári; Saba Khatatneh; Csaba Sőti

doi:10.3390/cells11162479

Hsp90: From Cellular to Organismal Proteostasis

Cells. 2022 Aug 10;11(16):2479. doi: 10.3390/cells11162479.

Authors

Milán Somogyvári¹, Saba Khatatneh¹, Csaba Sőti¹

Affiliation

¹ Department of Molecular Biology, Semmelweis University, H-1085 Budapest, Hungary.

Abstract

Assuring a healthy proteome is indispensable for survival and organismal health. Proteome disbalance and the loss of the proteostasis buffer are hallmarks of various diseases. The essential molecular chaperone Hsp90 is a regulator of the heat shock response via HSF1 and a stabilizer of a plethora of signaling proteins. In this review, we summarize the role of Hsp90 in the cellular and organismal regulation of proteome maintenance.

Keywords: Hsp90; aging; cancer; chaperones; development; neurodegenerative disease; obesity; proteostasis; stress.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

HSP90 Heat-Shock Proteins / metabolism
Heat-Shock Response
Molecular Chaperones / metabolism
Proteome* / metabolism
Proteostasis*

Substances

HSP90 Heat-Shock Proteins
Molecular Chaperones
Proteome

Grants and funding

This work was funded by grants from the Hungarian Science Foundation (OTKA K116525) to C.S., from the Department of Molecular Biology of the Semmelweis University (Intézeti Kutatási Bátorítás) to M.S. The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.