# HSP90 multi-functionality in cancer

## TL;DR

This paper explores how HSP90 proteins support cancer progression and how targeting them could lead to new cancer treatments.

## Contribution

The paper highlights the multi-functional role of HSP90 in promoting cancer hallmarks and its potential as a therapeutic target.

## Key findings

- HSP90 supports cancer by enabling cell death resistance and replicative immortality.
- HSP90 family members contribute to tumor immunity, angiogenesis, and metastasis.
- HSP90 inhibitors and vaccines are being developed as potential cancer therapies.

## Abstract

The 90-kDa heat shock proteins (HSP90s) are molecular chaperones essential for folding, unfolding, degradation and activity of a wide range of client proteins. HSP90s and their cognate co-chaperones are subject to various post-translational modifications, functional consequences of which are not fully understood in cancer. Intracellular and extracellular HSP90 family members (HSP90α, HSP90β, GRP94 and TRAP1) promote cancer by sustaining various hallmarks of cancer, including cell death resistance, replicative immortality, tumor immunity, angiogenesis, invasion and metastasis. Given the importance of HSP90 in tumor progression, various inhibitors and HSP90-based vaccines were developed for the treatment of cancer. Further understanding of HSP90 functions in cancer may provide new opportunities and novel therapeutic strategies for the treatment of cancer.