Co-chaperones: regulated action in conformational functions of HSP90 and their actions in cancer / 药学学报

Heat shock protein 90(HSP90), as an essential molecular chaperone, regulates the folding, assembly and maturation of a wide range of oncogenic client proteins. The process of adenosine triphosphate(ATP)binding and adenosine diphosphate(ADP)/ATP exchange act as a conformational switch to regulate the chaperone function of HSP90. Furthermore, this process is controlled by a range of accessory proteins(as referred to co-chaperones), such as Hop, CDC37, p23, AHA1, PP5, etc. This article describes the structure and function of several co-chaperones, and their roles in tumor progress.