Areas of Interest
Heat shock protein 90 (Hsp90) is a molecular chaperone that ensures proteostasis of over 400 “client” proteins in normal and cancer cells. In cancer cells, Hsp90 expression is increased and its function becomes crucial in maintaining various hallmarks of cancer. A number of proteins required to sustain these oncogenic characteristics are clients of Hsp90. Therefore, by extension, inhibition of Hsp90 will simultaneously knockdown multiple oncogenic signaling pathways.
My project focuses on inhibiting Hsp90 to overcome difficult-to-treat drug resistant melanomas. More specifically I am interested in understanding the genetic underpinnings of resistance pathways to improve treatment options for patients. Our novel inhibitors target the carboxy terminus (C-terminal) of the chaperone decreasing adverse effects that plague all other Hsp90 inhibitors tested in clinical trials. We hypothesize that C-terminal inhibition of Hsp90 will simultaneously inhibit resistance pathways to rescue these drug resistant melanomas.