期刊
出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2211258120
关键词
blister; endosomal trafficking; retromer; vacuolar protein transport
资金
- National Natural Science Foundation of China [32061160467, 31870171]
- NSFC [32000365, 31870301]
- Guangdong Province grant [2022A1515010913]
- China Postdoctoral Science Foundation [2021M691092, 2019M662950]
- Youth project of basic and applied basic research project of Guangdong Province [2021A1515110423]
- US National Science Foundation grant NSF [MCB 2114603]
The study identifies a plant-specific endosomal regulator, BLISTER (BLI), that interacts with the retromer complex and plays a crucial role in regulating endosomal trafficking in plants.
The retromer is a heteromeric protein complex that localizes to endosomal membranes and drives the formation of endosomal tubules that recycle membrane protein cargoes. In plants, the retromer plays essential and canonical functions in regulating the transport of vacuolar storage proteins and the recycle of endocytosed plasma membrane proteins (PM); however, the mechanisms underlying the regulation of assembly, protein stability, and membrane recruitment of the plant retromer complex remain to be elucidated. In this study, we identify a plant-unique endosomal regulator termed BLISTER (BLI), which colocalizes and associates with the retromer complex by interacting with the retromer core subunits VPS35 and VPS29. Depletion of BLI perturbs the assembly and membrane recruitment of the retromer core VPS26-VPS35-VPS29 trimer. Consequently, depletion of BLI disrupts retromer-regulated endosomal trafficking function, including transport of soluble vacuolar proteins and recycling of endocytosed PIN-FORMED (PIN) proteins from the endosomes back to the PM. Moreover, genetic analysis in Arabidopsis thaliana mutants reveals BLI and core retromer interact genetically in the regulation of endosomal trafficking. Taken together, we identified BLI as a plant-specific endosomal regulator, which functions in retromer pathway to modulate the recycling of endocytosed PM proteins and the trafficking of soluble vacuolar cargoes.
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