ArticleBiophysical journal2021
Improving the flexibility of genetically encoded voltage indicators via intermolecular FRET.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Noise Sources and Strategies for Signal Quality Improvement in Biological Imaging: A Review Focused on Calcium and Cell Membrane Voltage Imaging.Biosensors · 2026Review
- Modulating Chromophore Flexibility in GEVIs through Threonine-Based Molecular Switches Reveals an Influence of Membrane Curvature on Protein Activity.ACS sensors · 2025Article
- From Plankton to Primates: How VSP Sequence Diversity Shapes Voltage Sensing.International journal of molecular sciences · 2025Article
- Hydrophobic residues in S1 modulate enzymatic function and voltage sensing in voltage-sensing phosphatase.The Journal of general physiology · 2024Article
- Fluorescent Reporters for Sensing Membrane Potential: Tools for Bioelectricity.Bioelectricity · 2022Article
- Conserved Amino Acids Residing Outside the Voltage Field Can Shift the Voltage Sensitivity and Increase the Signal Speed and Size ofFrontiers in cell and developmental biology · 2022Article
- Advances and prospects of rhodopsin-based optogenetics in plant research.Plant physiology · 2021Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new family of genetically encoded voltage indicators (GEVIs) has been developed based on intermolecular Förster resonance energy transfer (FRET). To test the hypothesis that the GEVI ArcLight functions via interactions between the fluorescent protein (FP) domains of neighboring probes, the FP of ArcLight was replaced with either a FRET donor or acceptor FP. We discovered relatively large FRET signals only when cells were cotransfected with both the FRET donor and acceptor GEVIs. Using a cyan fluorescent protein donor and an RFP acceptor, we were able to observe a voltage-dependent signal with an emission peak separated by over 200 nm from the excitation wavelength. The intermolecular FRET strategy also works for rhodopsin-based probes, potentially improving their flexibility as well. Separating the FRET pair into two distinct proteins has important advantages over intramolecular FRET constructs. The signals are larger because the voltage-induced conformational change moves two FPs independently. The expression of the FRET donor and acceptor can also be restricted independently, enabling greater cell type specificity as well as refined subcellular voltage reporting.
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Registered trials
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