The molecular chaperone HSP-90 supports the folding, stability and function of numerous proteins involved in cellular signaling and regulation. Understanding its interaction network is therefore essential for uncovering how protein homeostasis contributes to physiological adaptation.
In this project, we aim to map the HSP-90-associated protein network in Caenorhabditis elegans. We use an inducible HSP-90–TurboID proximity-labeling system combined with affinity enrichment and mass spectrometry to identify proteins in the molecular environment of HSP-90. By comparing different experimental conditions, including pharmacological inhibition of HSP-90, we investigate changes in this network and select candidate interactions for further validation. Our goal is to identify established and previously unrecognized links between HSP-90, cellular stress responses and metabolism.
Responsible: Milán Somogyvári