生物
蛋白酶体
热应力
细胞生物学
计算生物学
生物化学
动物科学
作者
Zhouli Xie,Shuai Zhao,Yuchen Tu,Enhui Liu,Ying Li,Xingwei Wang,Changtian Chen,Shengxi Zhai,Jie Qi,Chengyun Wu,Honghong Wu,Mian Zhou,Wei Wang
标识
DOI:10.1016/j.molcel.2024.07.033
摘要
Stress granules (SGs) are conserved reversible cytoplasmic condensates enriched with aggregation-prone proteins assembled in response to various stresses. How plants regulate SG dynamics is unclear. Here, we show that 26S proteasome is a stable component of SGs, promoting the overall clearance of SGs without affecting the molecular mobility of SG components. Increase in either temperature or duration of heat stress reduces the molecular mobility of SG marker proteins and suppresses SG clearance. Heat stress induces dramatic ubiquitylation of SG components and enhances the activities of SG-resident proteasomes, allowing the degradation of SG components even during the assembly phase. Their proteolytic activities enable the timely disassembly of SGs and secure the survival of plant cells during the recovery from heat stress. Therefore, our findings identify the cellular process that de-couples macroscopic dynamics of SGs from the molecular dynamics of its constituents and highlights the significance of the proteasomes in SG disassembly.
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