Journal
CELL REPORTS
Volume 30, Issue 2, Pages 583-+Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2019.12.037
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Funding
- University of Turku
- Abo Akademi University
- Biocenter Finland
- Academy of Finland
- Sigrid Juselius Foundation
- Turku Doctoral Network in Molecular Biosciences
- Finnish Cultural Foundation
- Cancer Foundation Finland
- Abo Akademi University Research Foundation
- Magnus Ehrnrooth Foundation
- Tor, Joe and Pentti Borg Memory Foundation
- Ida Montin's Foundation
- Otto A. Malm Foundation
- Medical Research Foundation Liv och Halsa
- K. Albin Johansson's Foundation
- Agence Nationale Recherche [SAMENTA ANR-13-SAMA-0008-01]
- Short Researcher Mobility France Embassy/MESRI-Finnish Society of Science and Letters
- CNRS/Project International de Cooperation Scientifique PICS 2013-2015
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Maintenance of protein homeostasis, through inducible expression of molecular chaperones, is essential for cell survival under protein-damaging conditions. The expression and DNA-binding activity of heat shock factor 2 (HSF2), a member of the heat shock transcription factor family, increase upon exposure to prolonged proteotoxicity. Nevertheless, the specific roles of HSF2 and the global HSF2-dependent gene expression profile during sustained stress have remained unknown. Here, we found that HSF2 is critical for cell survival during prolonged proteotoxicity. Strikingly, our RNA sequencing (RNA-seq) analyses revealed that impaired viability of HSF2-deficient cells is not caused by inadequate induction of molecular chaperones but is due to marked downregulation of cadherin superfamily genes. We demonstrate that HSF2-dependent maintenance of cadherin-mediated cell-cell adhesion is required for protection against stress induced by proteasome inhibition. This study identifies HSF2 as a key regulator of cadherin superfamily genes and defines cell-cell adhesion as a determinant of proteotoxic stress resistance.
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