HSF1

Strain DNY75 expressing either human HSF1 (+HSF1) or an empty vector (+vector) were seeded into microtiter wells and incubated in the presence of HSF1A or DMSO solvent for 4 d and then photographed.

PLoS Biology: New Articles Daniel W. Neef et al. 2010

In addition, since HSF1 is repressed through an interaction with Hsp90, small molecule inhibitors of Hsp90 are often identified as HSF1-activating molecules

PLoS Biology: New Articles Daniel W. Neef et al. 2010

HSF1A stimulates human HSF1 multimerization in yeast and activates human HSF1-dependent yeast cell growth.

PLoS Biology: New Articles Daniel W. Neef et al. 2010

Although the association of HSF1 with protein chaperones is one mechanism for its regulation, HSF1 is also thought to engage in intramolecular coiled-coil interactions that maintain the monomeric state and point mutations in these coiled-coil domains (leucine zippers) cause constitutive multimerization when expressed in mammalian cells

PLoS Biology: New Articles Daniel W. Neef et al. 2010

Although the precise mechanisms underlying this defect in HSF1 activation are not clear, this could, in part, explain the selective sensitivity of neuronal cells in neurodegenerative diseases in which misfolded proteins are expressed in all tissues

PLoS Biology: New Articles Daniel W. Neef et al. 2010

In addition, we show that HSF1A interacts with components of the TRiC/CCT complex, suggesting a potentially novel regulatory role for this complex in modulating HSF1 activity.

PLoS Biology: New Articles Daniel W. Neef et al. 2010

The scientists further explored one of the candidate molecules to activate the master regulator of chaperone gene expression, Heat Shock Factor 1 (HSF1), to learn whether it would work in model systems of Huntington's disease, a devastating neurodegenerative disease of protein misfolding.

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Through these studies, we have identified HSF1A, a molecule capable of activating human HSF1, increasing the levels of protein chaperones and alleviating the toxicity of misfolded proteins in both cell culture as well as fruit fly models of neurodegenerative disease.

PLoS Biology: New Articles Daniel W. Neef et al. 2010

The damage to early-state rat neurons was much lower in cells pre-treated with the HSF1 activator, and damage to the neurons of fruit flies that had a Huntington's-like disorder was also greatly reduced.

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However, these screens often result in the identification of compounds that promote HSF1 activation through the proteotoxic accumulation of unfolded proteins or through the inhibition of Hsp90, a central chaperone involved in cell growth, signaling, and proliferation

PLoS Biology: New Articles Daniel W. Neef et al. 2010