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The highly heat-inducible HspA6 and the thermolabile DnaJB5 are potent regulators of heat shock transcription factor 1 activity.
Proceedings of the National Academy of Sciences · · Journal Article
Koch, Huo + more
Abstract ↗AI summary
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HspA6 is the most efficient cytonuclear Hsp70 for monomerizing Hsf1 with DnaJB1, while only DnaJB1, DnaJB4, and DnaJB5 support Hsf1 monomerization among class A/B JDPs.
- Why it matters: It remains unclear whether Hsf1 feedback control is specific to the HspA8–DnaJB1 pair or reflects a broader, isoform- and JDP-selective Hsp70 network regulating the heat shock response.
- What they did: The study tested Hsf1 monomerization by multiple cytonuclear Hsp70s and JDPs, assessed dependence on the Hsp70 EEVD motif, used HeLa cells for HSR readouts, and examined DnaJB5 behavior after temperature upshift.
- The result: EEVD-deleted HspA8 and HspA6 down-regulate the HSR in HeLa cells, DnaJB5 knockdown reduces HspA8–Hsf1 interaction, and heat upshift causes DnaJB5 to partially unfold and partition insolubly, implying increased Hsf1 activity.
The findingWhy it mattersWhat they didThe result
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