Heat shock proteins and cancer: The FoxM1 connection

Heat shock proteins (Hsp) and FoxM1 have significant roles in carcinogenesis. According to their relative molecular weight, Hsps are divided into Hsp110, Hsp90, Hsp70, Hsp60, Hsp40, and small Hsps. Hsp70 can play essential functions in cancer initiation and is overexpressed in several human cancers. Hsp70, in combination with cochaperones HIP and HOP, refolds partially denatured proteins and acts as a cochaperone for Hsp90. Also, Hsp70, in combination with BAG3, regulates the FoxM1 signaling pathway. FoxM1 protein is a transcription factor of the Forkhead family that is overexpressed in most human cancers and is involved in many cancers' development features, including proliferation, migration, invasion, angiogenesis, metastasis, and resistance to apoptosis. This review discusses the Hsp70, Hsp90, and FoxM1 structure and function, the known Hsp70 cochaperones, and Hsp70, Hsp90, and FoxM1 inhibitors.

Automated summary

Heat shock proteins (Hsps), including Hsp70, Hsp90, and small Hsps, and the transcription factor FoxM1, have important roles in carcinogenesis. Hsp70 functions in cancer initiation and protein folding, and is overexpressed in human cancers. It also interacts with cochaperones and regulates the FoxM1 signaling pathway. FoxM1 is overexpressed in most human cancers and is involved in various cancer-related processes. This review covers the structure, function, and inhibitors of Hsp70, Hsp90, and FoxM1.