应力颗粒
细胞生物学
化学
泛素
突变体
泛素连接酶
压力(语言学)
蛋白质降解
蛋白酶体
生物
热休克蛋白
综合应力响应
作者
Youngdae Gwon,Brian A. Maxwell,Regina-Maria Kolaitis,Peipei Zhang,Hong Joo Kim,Taylor Jp
标识
DOI:10.1101/2021.04.22.440930
摘要
Abstract Stress granules are dynamic, reversible condensates composed of RNA and protein that assemble in response to a variety of stressors and are normally disassembled after stress is removed. Whereas the composition of stress granules and the mechanisms underlying their assembly have been extensively studied, far less is known about the mechanisms that govern disassembly. Impaired disassembly has been implicated in some diseases. Here we report that stress granule disassembly is context-dependent and, in the setting of heat shock, requires ubiquitination of G3BP1, the central protein within the stress granule RNA-protein network. Ubiquitinated G3BP1 interacts with the ER-resident protein FAF2, which engages the ubiquitin-dependent segregase p97/VCP. Targeting G3BP1 enables the stress granule-specific interaction network to fall below the percolation threshold for phase separation, which causes disassembly. One Sentence Summary Ubiquitination of G3BP1 mediates FAF2- and p97/VCP-dependent disassembly of heat-induced stress granules
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