Regulation of Hsf1 and the Heat Shock Response
Regulation of Hsf1 and the Heat Shock Response
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DOI：
10.1007/978-3-030-40204-4_3
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发表时间：
2020-01-01
期刊：
影响因子：
--
通讯作者：
Pincus, David
中科院分区：
文献类型：
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作者：
Pincus, David
热休克反应（HSR）的特点是在温度突然升高后诱导分子伴侣。在真核生物中，HSR包含由转录因子Hsf1控制的一组基因。HSR是由共翻译蛋白质折叠、核糖体生物合成、新生蛋白质的细胞器靶向和泛素蛋白酶体系统的蛋白质降解缺陷诱导的。在热休克时，这些过程可能是激活HSR的多肽配体的内源性来源。从机制上讲，这些配体被认为是滴定分子伴侣Hsp70远离Hsf1，释放Hsf1诱导细胞分子伴侣的全部武库，以恢复蛋白质稳态。在后生动物中，这种细胞自主反馈回路由微环境和神经元线索调节，以实现组织水平和生物体范围的协调。
The heat shock response (HSR) is characterized by the induction of molecular chaperones following a sudden increase in temperature. In eukaryotes, the HSR comprises the set of genes controlled by the transcription factor Hsf1. The HSR is induced by defects in co-translational protein folding, ribosome biogenesis, organellar targeting of nascent proteins, and protein degradation by the ubiquitin proteasome system. Upon heat shock, these processes may be endogenous sources of polypeptide ligands that activate the HSR. Mechanistically, these ligands are thought to titrate the chaperone Hsp70 away from Hsf1, releasing Hsf1 to induce the full arsenal of cellular chaperones to restore protein homeostasis. In metazoans, this cell-autonomous feedback loop is modulated by the microenvironment and neuronal cues to enable tissue-level and organism-wide coordination.