ArticleThe Plant journal : for cell and molecular biology2014
Significant reduction of BiFC non-specific assembly facilitates in planta assessment of heterotrimeric G-protein interactors.
Article in The Plant journal : for cell and molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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84 citing papers in PubMed, 162 citations in OpenAlex.
- AHG1-AFP interaction as a regulatory node in the ABA response during seed germination.The Plant journal : for cell and molecular biology · 2026Article
- Introduction of the Ribo-BiFC method to plants using a split mVenus approach.Plant methods · 2026Article
- Phosphovariants of the canonical heterotrimeric Gα protein, GPA1, differentially affect G protein activity and Arabidopsis development.bioRxiv : the preprint server for biology · 2026Article
- SUPPRESSOR OF LAZY QUADRUPLE 1 acts at ER-plasma membrane contact sites to control a gravitropism pathway in theProceedings of the National Academy of Sciences of the United States of America · 2025Article
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- Comprehensive Review on Bimolecular Fluorescence Complementation and Its Application in Deciphering Protein-Protein Interactions in Cell Signaling Pathways.Biomolecules · 2024Review
- Improved validation of protein interactions using bicistronic BiFC (Bi2FC).Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
- Exogenous abscisic acid represses rice flowering via SAPK8-ABF1-Ehd1/Ehd2 pathway.Journal of advanced research · 2024Article
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- Discovering Dynamic Plant Enzyme Complexes in Yeast for Kratom Alkaloid Pathway Identification.Angewandte Chemie (International ed. in English) · 2023Article
- ABF1 Positively Regulates Rice Chilling Tolerance via Inducing Trehalose Biosynthesis.International journal of molecular sciences · 2023Article
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- Maize domestication phenotypes reveal strigolactone networks coordinating grain size evolution with kernel-bearing cupule architecture.The Plant cell · 2023Article
- A Nimble Cloning-compatible vector system for high-throughput gene functional analysis in plants.Plant communications · 2023Article
- Discovering dynamic plant enzyme complexes in yeast for novel alkaloid pathway identification from a medicinal plant kratom.bioRxiv : the preprint server for biology · 2023Article
- BRXL4-LAZY1 interaction at the plasma membrane controls Arabidopsis branch angle and gravitropism.The Plant journal : for cell and molecular biology · 2023Article
24 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Protein networks and signaling cascades are key mechanisms for intra- and intercellular signal transduction. Identifying the interacting partners of a protein can provide vital clues regarding its physiological role. The bimolecular fluorescence complementation (BiFC) assay has become a routine tool for in vivo analysis of protein-protein interactions and their subcellular location. Although the BiFC system has improved since its inception, the available options for in planta analysis are still subject to very low signal-to-noise ratios, and a systematic comparison of BiFC confounding background signals has been lacking. Background signals can obscure weak interactions, provide false positives, and decrease confidence in true positives. To overcome these problems, we performed an extensive in planta analysis of published BiFC fragments used in metazoa and plants, and then developed an optimized single vector BiFC system which utilizes monomeric Venus (mVenus) split at residue 210, and contains an integrated mTurquoise2 marker to precisely identify transformed cells in order to distinguish true negatives. Here we provide our streamlined double ORF expression (pDOE) BiFC system, and show that our advance in BiFC methodology functions even with an internally fused mVenus210 fragment. We illustrate the efficacy of the system by providing direct visualization of Arabidopsis MLO1 interacting with a calmodulin-like (CML) protein, and by showing that heterotrimeric G-protein subunits Gα (GPA1) and Gβ (AGB1) interact in plant cells. We further demonstrate that GPA1 and AGB1 each physically interact with PLDα1 in planta, and that mutation of the so-called PLDα1 'DRY' motif abolishes both of these interactions.
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