Ubiquitination is essential for recovery of cellular activities after heat shock.
Ubiquitination is essential for recovery of cellular activities after heat shock.
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DOI：
10.1126/science.abc3593
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发表时间：
2021-06-25
期刊：
影响因子：
--
通讯作者：
Taylor JP
中科院分区：
文献类型：
--
作者：
Maxwell BA;Gwon Y;Mishra A;Peng J;Nakamura H;Zhang K;Kim HJ;Taylor JP
真核细胞通过适应性程序对应激作出反应，包括关键细胞过程的可逆关闭、应激颗粒的形成以及泛素化的整体增加。这种泛素化的主要功能被认为是标记受损或错误折叠的蛋白质以进行降解。在这里，我们在哺乳动物培养细胞中进行研究，发现不同的压力会引发不同的泛素化模式。对于热应激，泛素化靶向与应激期间下调的细胞活动相关的特定蛋白质，包括核细胞质运输和翻译，以及应激颗粒成分。泛素化对于这些过程的关闭或应激颗粒的形成不是必需的，但对于细胞活动的恢复和应激颗粒的分解是必需的。因此，应激诱导的泛素化使细胞在热应激后恢复。应激诱导的泛素化对于热应激后细胞活动的恢复至关重要。
Eukaryotic cells respond to stress via adaptive programs that include reversible shutdown of key cellular processes, the formation of stress granules, and a global increase in ubiquitination. The primary function of this ubiquitination is thought to be for tagging damaged or misfolded proteins for degradation. Here, working in mammalian cultured cells, we found that different stresses elicited distinct ubiquitination patterns. For heat stress, ubiquitination targeted specific proteins associated with cellular activities downregulated during stress, including nucleocytoplasmic transport and translation, as well as stress granule constituents. Ubiquitination was not required for the shutdown of these processes or for stress granule formation but was essential for the resumption of cellular activities and for stress granule disassembly. Thus, stress-induced ubiquitination primes the cell for recovery following heat stress. Stress-induced ubiquitination is essential for recovery of cellular activities following heat stress.
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