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Aha-type co-chaperones: the alpha or the omega of the Hsp90 ATPase cycle?

机译:AHA型共伴侣:HSP90 ATPase循环的alpha或Ω

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摘要

Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that plays an essential role in cellular homeostasis. It functions in the context of a structurally dynamic ATP-dependent cycle to promote conformational changes in its clientele to aid stability, maturation, and activation. The client activation cycle is tightly regulated by a cohort of co-chaperone proteins that display specific binding preferences for certain conformations of Hsp90, guiding Hsp90 through its functional ATPase cycle. Aha-type co-chaperones are well-known to robustly stimulate the ATPase activity of Hsp90 but other roles in regulating the functional cycle are being revealed. In this review, we summarize the work done on the Aha-type co-chaperones since the 1990s and highlight recent discoveries with respect to the complexity of Hsp90 cycle regulation.
机译:热休克蛋白90(HSP90)是一种二聚体分子伴侣,其在细胞稳态中起重要作用。 它在结构动态的ATP依赖周期的上下文中起作用,以促进其客户的构象变化以辅助稳定性,成熟和激活。 客户端激活循环通过群副伴侣蛋白质紧密调节,该族蛋白质显示器通过其功能ATP酶周期显示HSP90的某些构象,引导HSP90。 众所周知,AHA型共伴侣均可刺激HSP90的ATP酶活性,但正在揭示调节功能循环的其他作用。 在这篇综述中,我们总结了自20世纪90年代以来,从1990年代自20世纪90年代突出了AHA型共伴侣的工作以及关于HSP90周期调节的复杂性的最新发现。

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