HSP90 mediates the connection of multiple programmed cell death in diseases

• Published in: Cell death & disease Vol. 13; no. 11; p. 929
• Main Authors: Peng, Caiwang, Zhao, Fengyan, Li, Hengli, Li, Ling, Yang, Yantao, Liu, Fang
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 05.11.2022; Springer Nature B.V; Nature Publishing Group
• Subjects: 631/80/82; 692/699; Antibodies; Apoptosis; Apoptosis - physiology; Autophagy; Autophagy - genetics; Biochemistry; Biomedical and Life Sciences; Cancer; Cell Biology; Cell Culture; Cell cycle; Cell death; Cell division; Cellular stress response; Disease; Ferroptosis; Heat shock proteins; Homeostasis; HSP90 Heat-Shock Proteins - genetics; HSP90 Heat-Shock Proteins - metabolism; Hsp90 protein; Humans; Immunology; Kinases; Life Sciences; Medical research; Molecular Chaperones; Necroptosis; Review; Review Article; Steroids
• ISSN: 2041-4889; 2041-4889
• DOI: 10.1038/s41419-022-05373-9

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.