辅助分子伴侣对HSP90构象功能的调节及其在肿瘤中的作用

Co-chaperones: regulated action in conformational functions of HSP90 and their actions in cancer

摘要: 热休克蛋白90（heat shock protein 90，HSP90）作为一种重要的分子伴侣，参与调控众多原癌客户蛋白的折叠、装配和成熟，在肿瘤的发生发展中发挥重要作用。三磷酸腺苷（adenosine triphosphate，ATP）的结合和二磷酸腺苷（adenosine diphosphate，ADP）/ATP的交换是驱动HSP90分子伴侣构象循环的关键要素。其中一些辅助分子伴侣协助HSP90的构象循环过程，参与肿瘤恶性进展。本文对一些常见的辅助分子伴侣，如Hop、CDC37、p23、AHA1和PP5等的结构、功能及其协助HSP90参与肿瘤发生发展的过程进行综述。

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.