MED12 interacts with the heat‐shock transcription factor HSF1 and recruits CDK8 to promote the heat‐shock response in mammalian cells

Activated and promoter-bound heat-shock transcription factor 1 (HSF1) induces RNA polymerase II recruitment upon heat shock, this is facilitated by the core Mediator in Drosophila yeast. Another module, CDK8 kinase module (CKM), consisting of four subunits including MED12 CDK8, plays a negative or positive role regulation transcription; however, its involvement HSF1-mediated remains unclear. We herein demonstrated that HSF1 interacted with recruited to HSP70 promoter during shock mammalian cells. The activity (and paralog CDK19) promoted expression partly phosphorylating HSF1-S326 maintained proteostasis capacity. These results indicate an important for CKM protection cells against proteotoxic stress.