泛素
自噬
细胞生物学
应力颗粒
热休克蛋白
化学
翻译(生物学)
热冲击
颗粒(地质)
蛋白质生物合成
热休克蛋白90
热休克蛋白70
生物
生物化学
细胞凋亡
信使核糖核酸
基因
古生物学
作者
Brian A. Maxwell,Youngdae Gwon,Ashutosh Mishra,Junmin Peng,Hajime Nakamura,Ke Zhang,Hong Joo Kim,J. Paul Taylor
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2021-06-25
卷期号:372 (6549)
被引量:62
标识
DOI:10.1126/science.abc3593
摘要
Eukaryotic cells respond to stress through 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 that are down-regulated 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 after heat stress.
科研通智能强力驱动
Strongly Powered by AbleSci AI