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Article Dans Une Revue Cell Reports Année : 2020

Heat Shock Factor 2 Protects against Proteotoxicity by Maintaining Cell-Cell Adhesion

Résumé

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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Dates et versions

hal-02929926 , version 1 (06-01-2021)

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Jenny Joutsen, Alejandro Jose da Silva, Jens Christian Luoto, Marek Andrzej Budzynski, Anna Serafia Nylund, et al.. Heat Shock Factor 2 Protects against Proteotoxicity by Maintaining Cell-Cell Adhesion. Cell Reports, 2020, 30 (2), pp.583-597.e6. ⟨10.1016/j.celrep.2019.12.037⟩. ⟨hal-02929926⟩
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