Role of heat shock proteins in oncogenesis and strategy for treating cancers using Drosophila model

Abstract

A cluster of closely stored molecules that are engaged in different cellular processes is the mammalian HSP90 protein family. HSP90 works with HSP70 but is not dependent on the cochaperone of HSP90. HSPs are molecular chaperones required to fold, stabilize, and degrade proteins that are responsible for multiple tumor types. Hence targeting HSP90 and HSP70 presents a striking strategy for treating cancers. The present review article provides an overview of the structure, mode of action as well as role of HSP90 and HSP70. They are part of key regulatory processes that directly influence oncogenic pathways. As Drosophila melanogaster acts as an appropriate model system for research studies involving the above-stated disorders, emphasis has been put on summarizing some of the research studies in oncogenesis.