24 October 2020

Some components of regulatory networks can modify the impact of mutations to other components. For example, proteins that repress the activity of other proteins may also tend to repress the impacts of mutations. What are other rules that dictate whether one protein represses or enhances the impacts of mutations in another? To investigate rules that arise from regulatory relationships, my lab focuses on the network of proteins that are regulated by the protein-folding chaperone, Hsp90. Hsp90 modifies the impacts of mutations in many genes, sometimes dampening these impacts but more often exaggerating them. My lab’s goal is to predict which impacts of mutation will be repressed v. enhanced by Hsp90. In doing so we strive to reveal generic rules that explain how regulatory network structure contributes to epistasis.

Relevant Papers:
-Simple regulatory relationships predict direction of epistasis link
-Hsp90 interacts with mutations in diverse ways link