Source 1primary paper2018Nature Chemical Biology
Toolkit/miRFP720
miRFP720
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
miRFP720 is a monomeric near-infrared fluorescent protein reported in the cited study as the most red-shifted monomeric NIR fluorescent protein. It functions as a fluorescent component for reporter construction that can be imaged with reduced spectral interference from visible-range probes and blue-green optogenetic tools.
Usefulness & Problems
Why this is useful
miRFP720 is useful for multiplexed live-cell imaging designs that need spectral separation from CFP-YFP-class reporters and visible-light optogenetic systems. In the cited work, this NIR reporter space enabled simultaneous observation of Rac1 activity during optogenetic manipulation of Rac1 and supported a multiplexed setup that revealed ROCK-dependent antagonism between RhoA and Rac1.
Source:
miRFP720 is a near-infrared fluorescent protein reported as the most red-shifted monomeric member in this study. It supports construction of reporters that can be imaged with less spectral interference from visible-range tools.
Source:
building near-infrared fluorescent reporters
Source:
reducing spectral overlap with CFP-YFP imaging and blue-green optogenetic tools
Problem solved
It helps solve spectral overlap that limits concurrent use of multiple genetically encoded fluorescent probes and optogenetic actuators. The evidence supports this role at the level of reporter compatibility, not as a standalone sensor or actuator.
Source:
It helps address spectral overlap that limits simultaneous use of multiple genetically encoded probes and optogenetic tools.
Source:
spectral overlap among genetically encoded probes
Published Workflows
Objective: Develop a near-infrared FRET-based Rac1 biosensor and use it together with visible-spectrum biosensors and optogenetic control to directly image and perturb Rho GTPase signaling without problematic spectral overlap.
Why it works: The abstract states that the red-shifted miRFP720 and the fully NIR miRFP670-miRFP720 FRET pair enabled biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools, allowing simultaneous readout and perturbation.
Rac1 GTPase activity sensingRhoA-Rac1 antagonismRac1-GDI binding coordinationupstream Rac1 activationnear-infrared FRET biosensor designmultiplexed fluorescence imagingoptogenetic perturbation
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
fluorescenceTechniques
Computational DesignTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The available evidence indicates that miRFP720 is used through genetic expression as a fluorescent protein component in cells. The supplied text does not specify additional cofactors, expression hosts, delivery methods, or construct design details beyond its use in reporter construction and fluorescence imaging.
The supplied evidence does not provide quantitative photophysical properties, maturation behavior, brightness, photostability, or direct performance comparisons beyond the claim of being the most red-shifted monomeric NIR fluorescent protein in that study. The evidence also does not show that miRFP720 alone reports Rac1 activity or perturbs signaling, because those functions depend on specific biosensor and optogenetic construct architectures.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.
and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.
showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.
We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Approval Evidence
1 source1 linked approval claimfirst-pass slug mirfp720
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720
Source:
tool capabilitysupports
miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Source:
Comparisons
Source-backed strengths
The cited study describes miRFP720 as the most red-shifted monomeric NIR fluorescent protein reported there, which is a clear spectral positioning advantage. Its use in a near-infrared FRET-enabled multiplex imaging context was sufficient to support simultaneous imaging and optogenetic experiments involving Rho GTPase signaling.
Source:
described as the most red-shifted monomeric near-infrared fluorescent protein
Source:
compatible with multiplexing alongside CFP-YFP imaging and blue-green optogenetic tools
Ranked Citations
- 1.