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

Lei Pang, Yuanzhi Huang, Yilin He, Dong Jiang and Ruixi Li (lirx@sustech.edu.cn)
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Lei Pang: Southern University of Science and Technology
Yuanzhi Huang: Southern University of Science and Technology
Yilin He: Southern University of Science and Technology
Dong Jiang: Southern University of Science and Technology
Ruixi Li: Southern University of Science and Technology

Nature Communications, 2025, vol. 16, issue 1, 1-20

Abstract: Abstract 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 β subunit of adaptor protein (AP) -3 complex (AP-3β) 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-3β is rapidly recruited to SGs upon heat induction and plays a key role in disassembling SGs during stress recovery. Genetic evidences support that AP-3β 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.

Date: 2025
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DOI: 10.1038/s41467-025-57306-7

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