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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。
As an important chaperone, heat shock protein 90 (HSP90) is involved in the folding, assembly and maturation of many proto-oncoprotein clients and plays an important role in tumorigenesis and progression. The combination of adenosine triphosphate (ATP) binding and adenosine diphosphate (ATP) / ATP exchange is a key element driving the conformational loop of the HSP90 chaperone. Some of these accessory chaperones assist in the conformational cycle of HSP90 and are involved in the malignant progression of tumors. This review summarizes the structure and function of several common chaperones, such as Hop, CDC37, p23, AHA1 and PP5, and their roles in assisting HSP90 in tumorigenesis.