Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Nat Rev Microbiol. 2012 Oct;10(10):693-704. doi: 10.1038/nrmicro2875.
Heat shock protein 90 (HSP90) is an essential, abundant and ubiquitous eukaryotic chaperone that has crucial roles in protein folding and modulates the activities of key regulators. The fungal Hsp90 interactome, which includes numerous client proteins such as receptors, protein kinases and transcription factors, displays a surprisingly high degree of plasticity that depends on environmental conditions. Furthermore, although fungal Hsp90 levels increase following environmental challenges, Hsp90 activity is tightly controlled via post-translational regulation and an autoregulatory loop involving heat shock transcription factor 1 (Hsf1). In this Review, we discuss the roles and regulation of fungal Hsp90. We propose that Hsp90 acts as a biological transistor that modulates the activity of fungal signalling networks in response to environmental cues via this Hsf1-Hsp90 autoregulatory loop.
热休克蛋白 90(HSP90)是一种必需的、丰富的和普遍存在的真核伴侣蛋白,在蛋白质折叠中起着至关重要的作用,并调节关键调节剂的活性。真菌 HSP90 的相互作用组包括许多客户蛋白,如受体、蛋白激酶和转录因子,表现出惊人的高可塑性,这取决于环境条件。此外,尽管真菌 HSP90 水平在环境挑战后增加,但 HSP90 活性通过翻译后调节和涉及热休克转录因子 1(Hsf1)的自调节环来严格控制。在这篇综述中,我们讨论了真菌 HSP90 的作用和调节。我们提出,HSP90 作为一个生物晶体管,通过这个 Hsf1-HSP90 自调节环,根据环境线索调节真菌信号网络的活性。