Reactome | HSF1 is activated by phosphorylation, translocation to the nucleus, and trimerization

HSF1 is activated by phosphorylation, translocation to the nucleus, and trimerization

Stable Identifier

R-HSA-9857091

Type

Reaction [uncertain]

Species

Homo sapiens

Compartment

cytosol, nucleoplasm

ReviewStatus

3/5

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HSF1 is activated by phosphorylation, translocation to the nucleus, and trimerization

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During the mitochondrial unfolded protein response (mtUPR), HSF1 is activated by phosphorylation (Katiyar et al. 2020, also observed during heat shock in Sarge et al. 1993), translocation from the cytosol to the nucleus (Baler et al. 1993, Sarge et al. 1993, Sutandy et al. 2023, Katiyar et al. 2020), trimerization (Baler et al. 1993 and inferred from the mouse homolog in Sarge et al. 1993, Katiyar et al. 2020), and possible oxidation of two cysteine residues (Cys-35 and Cys-105, inferred from the mouse homolog in Anh and Thiele 2003) in an uncharacterized order of events. These alterations expose the DNA-binding domain of HSF1, causing HSF1 to bind DNA elements of target genes (Baler et al. 1993).

Literature References

PubMed ID	Title	Journal	Year
37286597	A cytosolic surveillance mechanism activates the mitochondrial UPR Sutandy, FXR, Gößner, I, Tascher, G, Münch, C	Nature	2023
32302062	HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response Katiyar, A, Fujimoto, M, Tan, K, Kurashima, A, Srivastava, P, Okada, M, Takii, R, Nakai, A	FEBS Open Bio	2020
8455624	Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1 Baler, R, Dahl, G, Voellmy, R	Mol. Cell. Biol.	1993