HSP90:FKBP4:PTGES3 binds HSF1 trimer

Stable Identifier
Reaction [binding]
Homo sapiens
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Under non-stress conditions monomeric HSF1 is sequestered in a HSP90-containing heterocomplex. FKBP4 (immunophilin) is one of the components of HSP90-chaperone machinery which was found to associate with trimeric, but not monomeric form of HSF1 (Guo Y et al. 2001). Multichaperone complex of HSP90:FKBP4:PKGES3 has been shown to associate with HSF1 trimer through its regulatory domain, and this is thought to repress HSF1 transcriptional activity (Guo Y et al. 2001).

Literature References
PubMed ID Title Journal Year
11583998 Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex

Voellmy, R, Pratt, WB, Smith, DF, Toft, DO, Guettouche, T, Guo, Y, Fenna, M, Boellmann, F

J. Biol. Chem. 2001
9222609 A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor

Hjermstad, S, Rimerman, RA, Smith, DF, Nair, SC, Toran, EJ, Smithgall, TE

Cell Stress Chaperones 1996
Orthologous Events
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