蛋白质毒性
细胞生物学
应力颗粒
生物
热休克蛋白
细胞保护
串扰
细胞质
信号转导
细胞应激反应
细胞凋亡
未折叠蛋白反应
蛋白质稳态
蛋白质聚集
伴侣(临床)
细胞
翻译(生物学)
遗传学
战斗或逃跑反应
基因
内质网
病理
物理
光学
信使核糖核酸
医学
作者
Akanksha Verma,Shoichiro Sumi,Mahendra Seervi
出处
期刊:Apoptosis
[Springer Nature]
日期:2021-05-12
卷期号:26 (7-8): 371-384
被引量:8
标识
DOI:10.1007/s10495-021-01678-w
摘要
Heat shock proteins (HSPs) are evolutionary conserved 'stress-response' proteins that facilitate cell survival against various adverse conditions. HSP-mediated cytoprotection was hitherto reported to occur principally in two ways. Firstly, HSPs interact directly or indirectly with apoptosis signaling components and suppress apoptosis. Secondly, through chaperon activity, HSPs suppress proteotoxicity and maintain protein-homeostasis. Recent studies highlight the interaction of HSPs with cytoplasmic stress granules (SGs). SGs are conserved cytoplasmic mRNPs granules that aid in cell survival under stressful conditions. We primarily aim to describe the distinct cell survival strategy mediated by HSPs as the crucial regulators of SGs assembly and disassembly. Based on the growing evidence, HSPs and associated co-chaperones act as important determinants of SG assembly, composition and dissolution. Under cellular stress, as a 'stress-coping mechanism', the formation of SGs reprograms protein translation machinery and modulates signaling pathways indispensable for cell survival. Besides their role in suppressing apoptosis, HSPs also regulate protein-homeostasis by their chaperone activity as well as by their tight regulation of SG dynamics. The intricate molecular signaling in and around the nexus of HSPs-SGs and its importance in diseases has to be unearthed. These studies have significant implications in the management of chronic diseases such as cancer and neurodegenerative diseases where SGs possess pathological functions.
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