热休克蛋白（Hsp）和FoxM1在癌变过程中扮演重要角色。根据分子量的大小，Hsps可分为Hsp110，Hsp90，Hsp70，Hsp60，Hsp40和小的Hsps。Hsp70在癌症引发中起到重要作用，并在多种人类癌症中过度表达。 Hsp70与辅助蛋白HIP和HOP结合，对部分变性的蛋白质进行再折叠，并作为Hsp90的辅助蛋白。此外，Hsp70与BAG3一起调节FoxM1信号通路。FoxM1蛋白是Forkhead家族的转录因子，大多数人类癌症中都有过度表达，与增殖，迁移，侵袭，血管生成，转移和抗凋亡等癌症发展特征有关。本文讨论了Hsp70，Hsp90和FoxM1的结构和功能，已知的Hsp70辅助蛋白，以及Hsp70，Hsp90和FoxM1的抑制剂。版权所有©2023年Elsevier Inc.发表。

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.Copyright © 2023. Published by Elsevier Inc.