Co-chaperones: regulated action in conformational functions of HSP90 and their actions in cancer
10.16438/j.0513-4870.2017-0020
- VernacularTitle:辅助分子伴侣对HSP90构象功能的调节及其在肿瘤中的作用
- Author:
Ni-na XUE
1
;
Jing JIN
1
;
Xiao-guang CHEN
1
Author Information
1. State Key Laboratory of Bioactive Substances and Functions of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100050, China
- Publication Type:REVIEWS
- Keywords:
cancer;
heat shock protein 90;
co-chaperone;
client protein;
adenosine triphosphate
- From:
Acta Pharmaceutica Sinica
2017;52(7):1085-1090
- CountryChina
- Language:Chinese
-
Abstract:
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.
