A Hemidesmosome-to-Cytoplasm Translocation of Small Heat Shock Proteins Provides Immediate Protection against Heat Stress
A Hemidesmosome-to-Cytoplasm Translocation of Small Heat Shock Proteins Provides Immediate Protection against Heat Stress
复制标题
小热休克蛋白的半桥粒到细胞质的易位提供了针对热应激的立即保护
DOI：
10.1016/j.celrep.2020.108410
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发表时间：
2020
期刊：
影响因子：
8.8
通讯作者：
Zhang Huimin
中科院分区：
文献类型：
--
作者：
Fu Rong;Huang Zhaohui;Li Huijun;Zhu Yi;Zhang Huimin
小热休克蛋白（sHSPs）是在应激反应中维持蛋白稳态的重要调节因子。本研究表明，在正常条件下，秀丽隐杆线虫表皮中组成性表达的HSP-43被储存在基础的秀丽隐杆线虫半粒体（cehd）中，并迅速释放到细胞质中，在热胁迫下发挥保护作用。在非应激情况下，与cehd的关联可保护HSP-43免受降解或毒性细胞质聚集。我们的研究揭示了基于易位的sHSPs通过半底粒工作的快速和特异性热休克反应。它刷新了我们对稳定细胞粘附的抗应力功能的认识，并提供了对sHSPs活动控制策略的见解。它还强调了细胞结构完整性对抗应力和损伤控制的重要性。
Small heat shock proteins (sHSPs) are important regulators for maintaining protein homeostasis in response to stresses. However, the strategies used by constitutively expressed sHSPs to control their activities in normal versus stressed conditions are still not fully understood, Here we show that the constitutively expressed HSP-43 in the C. elegans epidermis is stored within the basal C. elegans hemidesmosomes (CeHDs) under normal conditions and is rapidly released into the cytoplasm to exert protective functions upon heat stress. The association with CeHDs protects HSP-43 from degradation or toxic cytoplasmic aggregation in unstressed situations. Our study reveals a rapid and specific translocation-based heat shock response of the sHSPs working through hemidesmosomes. It refreshes our knowledge about the stress-resistant functions of stable cellular adhesions and provides insight into the activity-control strategies of sHSPs. It also underlines the importance of structural integrity of the cells on stress resistance and damage control.