ArticleScientific reports2022
Förster resonance energy transfer biosensors for fluorescence and time-gated luminescence analysis of rac1 activity.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- CXCL-CXCR2 signaling drives cancer-endothelium interactions in SCLC metastatic seeding.bioRxiv : the preprint server for biology · 2026Article
- Real-Time Visualization of Isoform-Specific RAF-KRAS Interactions in Living Cells Using FRET-BRET Hybrid Biosensors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Development of Time-Resolved Luminescence Measurement Instruments for Biosensing and Bioimaging - An Overview.Measurement : journal of the International Measurement Confederation · 2025Article
- Inhibition of Rho GEFs attenuates pulmonary fibrosis through suppressing myofibroblast activation and reprogramming profibrotic macrophages.Cell death & disease · 2025Article
- Fluorescence-Based Portable Assays for Detection of Biological and Chemical Analytes.Sensors (Basel, Switzerland) · 2023Review
- FRET Based Biosensor: Principle Applications Recent Advances and Challenges.Diagnostics (Basel, Switzerland) · 2023Review
- Pixel-by-pixel autofluorescence corrected FRET in fluorescence microscopy improves accuracy for samples with spatially varied autofluorescence to signal ratio.Scientific reports · 2023Article
- Review of Mn-Doped Semiconductor Nanocrystals for Time-Resolved Luminescence Biosensing/Imaging.ACS applied nano materials · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Genetically encoded, Förster resonance energy transfer (FRET) biosensors enable live-cell optical imaging of signaling molecules. Small conformational changes often limit the dynamic range of biosensors that combine fluorescent proteins (FPs) and sensing domains into a single polypeptide. To address this, we developed FRET and lanthanide-based FRET (LRET) biosensors of Rac1 activation with two key features that enhance sensitivity and dynamic range. For one, alpha helical linker domains separate FRET partners and ensure a large conformational change and FRET increase when activated Rac1 at the biosensor C-terminus interacts with an amino-terminal Rac binding domain. Incorporation of a luminescent Tb(III) complex with long (~ ms) excited state lifetime as a LRET donor enabled time-gated luminescence measurements of Rac1 activity in cell lysates. The LRET dynamic range increased with ER/K linker length up to 1100% and enabled robust detection of Rac1 inhibition in 96-well plates. The ER/K linkers had a less pronounced, but still significant, effect on conventional FRET biosensors (with FP donors and acceptors), and we were able to dynamically image Rac1 activation at cell edges using fluorescence microscopy. The results herein highlight the potential of FRET and LRET biosensors with ER/K linkers for cell-based imaging and screening of protein activities.
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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.