ArticleScientific reports2013
A new protein-protein interaction sensor based on tripartite split-GFP association.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.
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Who cites it
137 citing papers in PubMed.
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- Coiled-coil homo-oligomerization and disaggregase Hsp104 act in parallel to stabilize orphan septins.bioRxiv : the preprint server for biology · 2026Article
- Selection and evaluation of new sites for splitting beta-lactamase to modulate auto-complementation enzyme activity.Biochimica et biophysica acta. General subjects · 2026Article
- Article
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- Bipartite Genetically Encoded Biosensors to Sense Calcium Ion Dynamics at Membrane-Membrane Contact Sites.Analytical chemistry · 2025Article
- Design and evaluation of a tripartite chemogenetic fluorescent reporter for visualizing ternary protein complexes.Nature communications · 2025Article
- MyD88 polymerization and association to cellular membranes in a yeast heterologous model.Cellular and molecular life sciences : CMLS · 2025Article
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- Split genetically encoded calcium indicators for interorganellar junctions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Targeted disruption of PRC1.1 complex enhances bone remodeling.Nature communications · 2025Article
- Principles and Design of Molecular Tools for Sensing and Perturbing Cell Surface Receptor Activity.Chemical reviews · 2025Review
- Article
77 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors.
Funding
Abstract
Monitoring protein-protein interactions in living cells is key to unraveling their roles in numerous cellular processes and various diseases. Previously described split-GFP based sensors suffer from poor folding and/or self-assembly background fluorescence. Here, we have engineered a micro-tagging system to monitor protein-protein interactions in vivo and in vitro. The assay is based on tripartite association between two twenty amino-acids long GFP tags, GFP10 and GFP11, fused to interacting protein partners, and the complementary GFP1-9 detector. When proteins interact, GFP10 and GFP11 self-associate with GFP1-9 to reconstitute a functional GFP. Using coiled-coils and FRB/FKBP12 model systems we characterize the sensor in vitro and in Escherichia coli. We extend the studies to mammalian cells and examine the FK-506 inhibition of the rapamycin-induced association of FRB/FKBP12. The small size of these tags and their minimal effect on fusion protein behavior and solubility should enable new experiments for monitoring protein-protein association by fluorescence.
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