The adaptor protein AP-3β disassembles heat-induced stress granules via 19S regulatory particle in Arabidopsis

被引：0
作者：
Pang, Lei [1 ]
Huang, Yuanzhi [1 ]
He, Yilin [1 ]
Jiang, Dong [1 ]
Li, Ruixi [1 ]
机构：
[1] Southern Univ Sci & Technol, Inst Plant & Food Sci, Sch Life Sci, Dept Biol,Shenzhen Key Lab Plant Genet Engn & Mol, Shenzhen 518055, Peoples R China
来源：
NATURE COMMUNICATIONS | 2025年 / 16卷 / 01期
基金：
中国国家自然科学基金;
关键词：
PROCESSING BODIES; BREFELDIN-A; PREVACUOLAR COMPARTMENTS; PROTEASOME INHIBITOR; COMPLEX; POLYUBIQUITINATION; LOCALIZATION; INTERACTS; MECHANISM; TRANSIENT;
D O I：
10.1038/s41467-025-57306-7
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
To survive under adverse conditions, plants form stress granules (SGs) to temporally store mRNA and halt translation as a primary response. Dysregulation in SG disassembly can have detrimental effects on plant survival after stress release, yet the underlying mechanism remains poorly understood. Using Arabidopsis as a model system, we demonstrate that the beta subunit of adaptor protein (AP) -3 complex (AP-3 beta) interacts with the SG core RNA-binding proteins Tudor staphylococcal nuclease 1/2 (TSN1/2) both in vitro and in vivo. We also show that AP-3 beta is rapidly recruited to SGs upon heat induction and plays a key role in disassembling SGs during stress recovery. Genetic evidences support that AP-3 beta serves as an adaptor to recruit the 19S regulatory particle (RP) of the proteasome to SGs. Notably, the 19S RP promotes SG disassembly through RP-associated deubiquitylation, independent of its proteolytic activity. This deubiquitylation process of SG components is crucial for translation reinitiation and growth recovery after heat release. Our findings uncover a previously unexplored role of the 19S RP in regulating SG disassembly and highlights the importance of endomembrane proteins in supporting RNA granule dynamics in plants.
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页数：20
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