热休克蛋白90三磷酸腺苷酶的调控机制研究

热休克蛋白90（heat shock protein90，Hsp90）是一类在生物进化中高度保守的蛋白，与细胞凋亡密切相关，作为抗癌新靶标已经得到了广泛的关注。相关研究表明，Hsp90可以通过多种方式调控ATPase的活性，如自身构象改变、与辅伴侣分子形成复合物以及转录后修饰等。在Hsp90基本构象改变的基础上，综述了不同因素对ATPase的调控作用，着重阐述近几年的研究进展，为进一步研究Hsp90调控ATPase的机制提供一定的参考。

Study of the regulation mechanism of Hsp90 ATPase

As a conserved protein family, heat shock protein 90 （Hsp90） plays an important role in cell apoptosis. Hsp90 has emerged as an exciting target for cancer treatment. Hsp90 is responsible for regulating its ATPase activity by a variety of ways, including structural changes of Hsp90, co-chaperone modulations and post-translation modifications. In this review, we describe the conformation changes of Hsp90, summarize the different regulation mechanism of Hsp90 ATPase activity, and highlight the recent research progress.