ArticleNature communications2025
Pupylation-based proximity labeling reveals regulatory factors in cellulose biosynthesis in Arabidopsis.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Application of Proximity-Labeling Techniques in Plants: A Review of Successful Cases.International journal of molecular sciences · 2026Review
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
- Controlling distance, time and reactivity: Chemical principles of proximity labeling.Current opinion in chemical biology · 2026Review
- Accelerating Resistance Breeding: Emerging Methods to Identify and Validate Plant Immunity Genes.Plants (Basel, Switzerland) · 2026Review
- RACK1A interacts and colocalizes with FSD1 in stress granules to regulate salt stress response in Arabidopsis.Plant physiology · 2026Article
- Capturing protein-protein interactions in plants: recent advances, challenges, and opportunities.Frontiers in molecular biosciences · 2026Review
- A plant-specific cytochromeScience advances · 2025Article
- The role of VND transcription factors in xylem vessel development and secondary wall formation.The New phytologist · 2025Review
- Pupylation-Based Proximity Labeling Unravels a Comprehensive Protein and Phosphoprotein Interactome of the Arabidopsis TOR Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Knowledge about how and where proteins interact provides a pillar for cell biology. Protein proximity-labeling has emerged as an important tool to detect protein interactions. Biotin-related proximity labeling approaches are by far the most commonly used but may have labeling-related drawbacks. Here, we use pupylation-based proximity labeling (PUP-IT) as a tool for protein interaction detection in plants. We show that PUP-IT readily confirmed protein interactions for several known protein complexes across different types of plant hosts and that the approach increased detection of specific interactions as compared to biotin-based proximity labeling systems. To further demonstrate the power of PUP-IT, we used the system to identify protein interactions of the protein complex that underpin cellulose synthesis in plants. Apart from known complex components, we identified the ARF-GEF BEN1 (BFA-VISUALIZED ENDOCYTIC TRAFFICKING DEFECTIVE1). We show that BEN1 contributes to cellulose synthesis by regulating both clathrin-dependent and -independent endocytosis of the cellulose synthesis protein complex from the plasma membrane. Our results highlight PUP-IT as a powerful proximity labeling system to identify protein interactions in plant cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.