ArticleProceedings of the National Academy of Sciences of the United States of America2023
A plant-unique protein BLISTER coordinates with core retromer to modulate endosomal sorting of plasma membrane and vacuolar proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- A MAP-SNARE interaction links cortical microtubules to the exocytic fusion machinery during auxin-dependent growth remodeling.Science advances · 2026Article
- Cu(I)-N-Heterocyclic carbenes as potent inhibitors of SARS-CoV-2 replication.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Article
- Post-Golgi Trafficking in Plant Cells.Sub-cellular biochemistry · 2026Review
- Plant-specific BLISTER modulates miRNA biogenesis by regulating MIR transcription, HYL1 phosphorylation, and nuclear transport in Arabidopsis.Nucleic acids research · 2025Article
- Vacuolar sorting receptors coordinate lytic vacuolar and autophagic transport for plant effector-triggered immunity.Nature plants · 2025Article
- Vacuolar protein sorting-associated protein Vps17 regulates sexual reproduction and virulence ofMycology · 2025Article
- Contrasting Retromer with a Newly Described Retriever inPlants (Basel, Switzerland) · 2024Review
- Arabidopsis retromer subunit AtVPS29 is involved in SLY1-mediated gibberellin signaling.Plant cell reports · 2024Article
- Diversity of retromer-mediated vesicular trafficking pathways in plants.Frontiers in plant science · 2023Review
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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