HSF1 phase transition mediates stress adaptation and cell fate decisions.

ABSTRACT: Under proteotoxic stress, some cells survive whereas others die. The mechanisms governing this heterogeneity in cell fate remain unknown. Here we report that condensation and phase transition of heat-shock factor 1 (HSF1), a transcriptional regulator of chaperones^1,2, is integral to cell-fate decisions underlying survival or death. During stress, HSF1 drives chaperone expression but also accumulates separately in nuclear stress bodies called foci^3-6. Foci formation has been regarded as a marker of cells actively upregulating chaperones^3,6-10. Using multiplexed tissue imaging, we observed HSF1 foci in human tumours. Paradoxically, their presence inversely correlated with chaperone expression. By live-cell microscopy and single-cell analysis, we found that fo

SUBMITTER: Gaglia G 

PROVIDER: S-EPMC7135912 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature