Heat shock master switch
Proteotoxic stress chaperone response
Also searched as Proteotoxic stress chaperone response.
You want it responsive: an active HSF1 program lets cells refold and rescue proteins under stress, and it tracks with longevity.
In depth
The master transcription factor of the heat-shock response — the sentinel that, sensing proteotoxic stress, mobilizes the cell's chaperone defenses.
What drives it
Longevity gene increases it.
Westerheide 2009, Science 323:1063 — SIRT1 deacetylates HSF1, sustaining its DNA-binding and prolonging the heat-shock response; links the SIRT1 longevity factor to proteostasis. PMID 19229036
Heat exposure increases it.
Åkerfelt 2010, Nat Rev Mol Cell Biol 11:545 — heat and proteotoxic stress activate HSF1, the master regulator that integrates cell stress with lifespan. doi 10.1038/nrm2938
Energy sensing reduces it.
The decrease in AMP/ATP ratio triggered by metformin is enough to activate AMPK, which in turn phosphorylates HSF1 and inhibits HSF1 DNA binding on heat shock response elements. 10.1083/jcb.201612006. doi 10.1083/jcb.201612006
What it drives
It increases Heat shock response.
Åkerfelt 2010, Nat Rev Mol Cell Biol 11:545 — HSF1 is the master transcription factor of the heat-shock response, inducing the molecular chaperones (heat-shock proteins). doi 10.1038/nrm2938
It increases Protein quality control.
HSF1 governs the heat-shock response and the chaperone network that maintains protein folding - 'HSF1 is the master regulator in vertebrates'. doi 10.1038/nrm2938
Blends that modulate it
Each blend page names this pathway and carries the study behind its claim.
See it on the map
Open the causal map to follow this pathway upstream and downstream, arrow by arrow, each with its study.