ArticleCell reports2016
RefSOFI for Mapping Nanoscale Organization of Protein-Protein Interactions in Living Cells.
Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
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- Molecular Spies in Action: Genetically Encoded Fluorescent Biosensors Light up Cellular Signals.Chemical reviews · 2024Review
- Comprehensive Review on Bimolecular Fluorescence Complementation and Its Application in Deciphering Protein-Protein Interactions in Cell Signaling Pathways.Biomolecules · 2024Review
- The Cytoplasmic Region of SARAF Reduces Triple-Negative Breast Cancer Metastasis through the Regulation of Store-Operated Calcium Entry.International journal of molecular sciences · 2023Article
- Fluorescence fluctuation-based super-resolution microscopy: Basic concepts for an easy start.Journal of microscopy · 2022Review
- Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor.Nature communications · 2022Article
- DrFLINC Contextualizes Super-resolution Activity Imaging.Journal of the American Chemical Society · 2021Article
- Seeing beyond the limit: A guide to choosing the right super-resolution microscopy technique.The Journal of biological chemistry · 2021Review
- Genetically Encoded Biosensors Based on Fluorescent Proteins.Sensors (Basel, Switzerland) · 2021Review
- Genetically Encodable Fluorescent and Bioluminescent Biosensors Light Up Signaling Networks.Trends in biochemical sciences · 2020Review
- Signaling diversity enabled by Rap1-regulated plasma membrane ERK with distinct temporal dynamics.eLife · 2020Article
- Recent advances in the use of genetically encodable optical tools to elicit and monitor signaling events.Current opinion in cell biology · 2020Review
- Septin2 mediates podosome maturation and endothelial cell invasion associated with angiogenesis.The Journal of cell biology · 2020Article
- Cusp-artifacts in high order superresolution optical fluctuation imaging.Biomedical optics express · 2020Article
- Fluorescent Protein-Based Indicators for Functional Super-Resolution Imaging of Biomolecular Activities in Living Cells.International journal of molecular sciences · 2019Review
- Single-molecule localization to study cytoskeletal structures, membrane complexes, and mechanosensors.Biophysical reviews · 2019Review
- Split Green Fluorescent Proteins: Scope, Limitations, and Outlook.Annual review of biophysics · 2019Review
- Genetically Encoded Fluorescent Biosensors Illuminate the Spatiotemporal Regulation of Signaling Networks.Chemical reviews · 2018Review
- FRET-enhanced photostability allows improved single-molecule tracking of proteins and protein complexes in live mammalian cells.Nature communications · 2018Article
- Live-cell imaging of cell signaling using genetically encoded fluorescent reporters.The FEBS journal · 2018Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
It has become increasingly clear that protein-protein interactions (PPIs) are compartmentalized in nanoscale domains that define the biochemical architecture of the cell. Despite tremendous advances in super-resolution imaging, strategies to observe PPIs at sufficient resolution to discern their organization are just emerging. Here we describe a strategy in which PPIs induce reconstitution of fluorescent proteins (FPs) that are capable of exhibiting single-molecule fluctuations suitable for stochastic optical fluctuation imaging (SOFI). Subsequently, spatial maps of these interactions can be resolved in super-resolution in living cells. Using this strategy, termed reconstituted fluorescence-based SOFI (refSOFI), we investigated the interaction between the endoplasmic reticulum (ER) Ca(2+) sensor STIM1 and the pore-forming channel subunit ORAI1, a crucial process in store-operated Ca(2+) entry (SOCE). Stimulating SOCE does not appear to change the size of existing STIM1/ORAI1 interaction puncta at the ER-plasma membrane junctions, but results in an apparent increase in the number of interaction puncta.
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