HSP90 mediates the connection of multiple programmed cell death in diseases

Heat shock protein (HSP) 90, an important component of the molecular chaperone network, is closely concerned with cellular signaling pathways and stress response by participating in the process of maturation and activation of client proteins, playing a crucial role both in the normal and abnormal operation of the organism. In functionally defective tissues, programmed cell death (PCD) is one of the regulable fundamental mechanisms mediated by HSP90, including apoptosis, autophagy, necroptosis, ferroptosis, and others. Here, we show the complex relationship between HSP90 and different types of PCD in various diseases, and discuss the possibility of HSP90 as the common regulatory nodal in multiple PCD, which would provide a new perspective for the therapeutic approaches in disease.

Automated summary

This article introduces the heat shock protein 90 (HSP90) as an important component of the molecular chaperone network, involved in cellular signaling pathways and stress response. It discusses the complex relationship between HSP90 and different types of programmed cell death (PCD) in various diseases, and proposes HSP90 as a potential common regulatory nodal for multiple PCD, offering a new perspective for disease therapies.