The ability to accurately sense and respond to danger is critical for survival. Environmental fluctuations can cause cellular damage, leading to protein misfolding and aggregation, which is toxic to cells. Cells can activate defense mechanisms like the Heat Shock Response to minimize protein damage by increasing production of protective proteins known as heat shock proteins (HSPs). These HSPs act as molecular chaperones to assist with the clearing out of damaged proteins. Chaperone expression is regulated by the conserved heat shock transcription factor (HSF-1).

Felicia's thesis was based on the discovery of innate mechanisms in organisms that coordinate activation of this cellular defense mechanism against protein misfolding. My research showed that the protective heat shock response in the cells of the animal could be triggered through serotonergic signaling, even in the absence of real damage. Additionally, Felicia showed that anticipation of danger can enhance the animal’s stress response in a serotonin-dependent manner, thus facilitating better survival against a subsequent insult that can cause protein damage.

Together, these studies allow for understanding how sensory inputs are coupled to gene expression under stressful conditions, and for characterization of the mechanisms by which animals adapt to changes in their environment by coordinating sensory input with changes in behavior and gene expression.