Mechanisms of Action of HSP110 and Its Cognate Family Members in Carcinogenesis

Tumors, as chronic malignant diseases that account for about 20% of all deaths worldwide, are the number one threat to human health. Until now there is no reliable treatment for most types of tumors. Tumorigenesis and cellular carcinogenesis remain difficult challenges due to their complex etiology and unknown mechanisms. As stress process regulating molecules and protein folding promoters, heat shock proteins (HSPs) play an important role in cancer development. Most studies have shown that HSPs are one of the major anticancer drug targets. HSPs are not only modulators of the cellular stress response, but are also closely associated with tumor initiation, progression, and drug resistance, so understanding the mechanism of the HSP family involved in cellular carcinogenesis is an important part of understanding tumorigenesis and enabling anticancer drug development. In this review, we discuss the functions and mechanisms of key members of the HSP family (HSP70, HSP90, and HSP110) in participating in the process of tumorigenesis and cell carcinogenesis, and look forward to the prospect of key members of the HSP family in targeted cancer therapy.