HSP70 Family in Cancer: Signaling Mechanisms and Therapeutic Advances

Biomolecules. 2023 Mar 27;13(4):601. doi: 10.3390/biom13040601.

Abstract

The 70 kDa heat shock proteins (HSP70s) are a group of highly conserved and inducible heat shock proteins. One of the main functions of HSP70s is to act as molecular chaperones that are involved in a large variety of cellular protein folding and remodeling processes. HSP70s are found to be over-expressed and may serve as prognostic markers in many types of cancers. HSP70s are also involved in most of the molecular processes of cancer hallmarks as well as the growth and survival of cancer cells. In fact, many effects of HSP70s on cancer cells are not only related to their chaperone activities but rather to their roles in regulating cancer cell signaling. Therefore, a number of drugs directly or indirectly targeting HSP70s, and their co-chaperones have been developed aiming to treat cancer. In this review, we summarized HSP70-related cancer signaling pathways and corresponding key proteins regulated by the family of HSP70s. In addition, we also summarized various treatment approaches and progress of anti-tumor therapy based on targeting HSP70 family proteins.

Keywords: HSP70; cancer; signaling pathway; treatment.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • HSP70 Heat-Shock Proteins* / metabolism
  • Heat-Shock Proteins / metabolism
  • Humans
  • Molecular Chaperones / metabolism
  • Neoplasms* / drug therapy
  • Protein Folding
  • Signal Transduction

Substances

  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones

Grants and funding

This study was supported by grants from the National Natural Science Foundation of China (Grant No. 82203153 to K.Z. and Grant No. 31771549 to Y.C.) and the Natural Science Foundation of Sichuan Province (Grant 2022NSFSC1438 to J.Z.).