Cells experience various proteotoxic stress, which causes severe damages unless managed by cellular stress responses. These include the heat shock response, hypoxic stress response, osmotic stress response, unfolded protein response, and oxidative stress response. A key regulator of cellular stress responses is the transcription factor family called heat shock factors (HSFs). One of the main interests in our laboratory is to understand the functions of HSF1 and HSF2 in response to distinct proteotoxic stresses, including oxidative stress, proteasome inhibition and repeated heat stress. We believe that depending on a cellular state, HSF1 and HSF2 can have various functions beyond the conventional heat shock response, which involves the inducible expression of heat shock proteins (Hsps). This idea is supported by many genome-wide screens performed by us and others, revealing that both HSF1 and HSF2 localize to promoters and other regulatory regions of several genes unrelated to chaperone machinery and protein folding. In order to uncover the functional impact of HSFs in different biological contexts, we utilize high-throughput methods such as ChIP-seq, PRO-seq, and RNA-seq (for details, see Methods).